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10-hydroxydodecanoic acid + glutathione + NAD+
?
-
-
-
-
?
12-hydroxydodecanoic acid + glutathione + NAD+
S-(11-carboxy)undecanyl-glutathione + NADH + H+
12-hydroxydodecanoic acid + glutathione + NAD+
S-(11-carboxy)undecanylglutathione + NADH
-
-
-
-
?
12-hydroxydodecanoic acid + NAD+
? + NADH
-
-
-
-
?
12-hydroxydodedecanoic acid + glutathione + NAD+
12-oxododecanoic acid + ?
3-ethoxy-2-hydroxybutyraldehyde + glutathione + NAD+
S-(3-ethoxy-2-hydroxybutyryl)-glutathione + NADH + H+
3-nitrotyrosine + NADPH + H+
? + NADP+
-
-
-
-
?
butanol + glutathione + NAD+
?
-
-
-
-
?
cinnamyl alcohol + glutathione + NAD+
S-cinnamylglutathione + NADH
-
-
-
-
?
decanol + glutathione + NAD+
?
-
-
-
-
?
farnesol + glutathione + NAD+
S-farnesylglutathione + NADH
-
-
-
-
?
formaldehyde + 6-mercaptohexanoate + NAD+
S-formyl-6-mercaptohexenoate + NADH
-
30% of the activity with glutathione
-
-
?
formaldehyde + 8-mercaptooctanoate + NAD+
S-formyl-8-mercaptooctanoate + NADH
-
35% of the activity with glutathione
-
-
?
formaldehyde + captopril + NAD+
S-formylcaptopril + NADH
-
8% of the activity with glutathione
-
-
?
formaldehyde + glutathione + 3-acetylpyridine-adenine dinucleotide
S-formylglutathione + ?
-
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
formaldehyde + glutathione + NADP+
S-formylglutathione + NADPH + H+
formaldehyde + glutathione + nicotinamide-hypoxanthine dinucleotide
S-formylglutathione + ?
-
-
-
-
?
formaldehyde + glutathione + thio-NAD+
S-formylglutathione + thio-NADH
-
-
-
-
?
formaldehyde + glutathione monomethyl ester + NAD+
S-formylglutathione monomethyl ester + NADH
-
70% of the activity with glutathione
-
-
?
formaldehyde + NAD+ + glutathione
S-formylglutathione + NADH
-
multifunctional enzyme, ADH3 constitutes a key enzyme in the detoxification of endogenous and exogenous formaldehyde, formaldehyde is released during intracellular metabolism of endogenous compounds or xenobiotics, expression of ADH3 might thus fulfill a protective role against DNA damage resulting from formaldehyde sources, ADH3 itself catalyzes oxidative reactions which produce NADH, most importantly the oxidation of formaldehyde
-
-
?
formaldehyde + S-hydroxymethyl glutathione + NAD+
?
geraniol + glutathione + NAD+
S-geranylglutathione + NADH
-
-
-
-
?
glyoxal + glutathione + NAD+
S-oxoacetylglutathione + NADH
hydroxypyruvaldehyde + glutathione + NAD+
S-hydroxypyruvylglutathione + NADH
methylglyoxal + glutathione + NAD+
S-pyruvylglutathione + NADH
metronidazole + NADPH + H+
? + NADP+
-
-
-
-
?
n-octanol + NAD+
n-octanal + NADH
-
-
-
-
?
nitrofurantoin + NADPH + H+
? + NADP+
-
-
-
-
?
nitrofurazone + NADPH + H+
? + NADP+
-
-
-
-
?
octanol + glutathione + NAD+
?
pentanol + glutathione + NAD+
?
-
-
-
-
?
pyruvylglutathione + NADH + H+
methylglyoxal + NAD+
-
-
-
-
r
S-(hydroxymethyl)glutathione + NAD(P)+
S-formylglutathione + NAD(P)H + H+
-
multifunctional enzyme, large active site pocket of enzyme entails special substrate specificities: short-chain alcohols are poor substrates, while medium-chain alcohols and particularly the glutathione adducts S-hydroxymethylglutathioneand S-nitrosoglutathione are efficiently converted, universal presence and structural conservation imply that ADH3 performs essential housekeeping functions in living organisms
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
S-formylglutathione + NADH
formaldehyde + glutathione + NAD+
S-formylglutathione + NADPH
formaldehyde + glutathione + NADP+
S-hydroxymethylglutathione + NAD+
S-formylglutathione + NADH + H+
S-nitrosocysteine + NADPH + H+
? + NADP+
-
-
-
-
?
S-nitrosoglutathione + NAD(P)H + H+
?
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
S-nitrosoglutathione + NADH
? + NAD+
S-nitrosoglutathione + NADH
GSH + NAD+ + NO
S-nitrosoglutathione + NADH + H+
?
S-nitrosoglutathione + NADH + H+
? + NAD+
S-nitrosoglutathione + NADH + H+
glutathione disulfide + hydroxylamine + NH4+ + NAD+
S-nitrosoglutathione + NADH + H+
GSH + NAD+ + NO
-
-
-
-
?
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
S-nitrosoglutathione + NADH + H+
GSSG + hydroxylamine + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
S-amino-L-glutathione + NAD+ + ?
S-nitrosoglutathione + NADPH + H+
? + NADP+
-
-
-
-
?
S-nitrosoglutathione + NADPH + H+
glutathione disulfide + hydroxylamine + NH4+ + NADP+
S-nitrosoglutathione + NADPH + H+
GSSG + ammonia + NADP+
S-pyruvylglutathione + NADH
methylglyoxal + glutathione + NAD+
-
-
-
?
additional information
?
-
12-hydroxydodecanoic acid + glutathione + NAD+
S-(11-carboxy)undecanyl-glutathione + NADH + H+
-
-
-
-
?
12-hydroxydodecanoic acid + glutathione + NAD+
S-(11-carboxy)undecanyl-glutathione + NADH + H+
-
best substrate for ADH3
-
-
?
12-hydroxydodedecanoic acid + glutathione + NAD+
12-oxododecanoic acid + ?
-
-
-
-
?
12-hydroxydodedecanoic acid + glutathione + NAD+
12-oxododecanoic acid + ?
-
-
-
?
12-hydroxydodedecanoic acid + glutathione + NAD+
12-oxododecanoic acid + ?
-
-
-
-
?
3-ethoxy-2-hydroxybutyraldehyde + glutathione + NAD+
S-(3-ethoxy-2-hydroxybutyryl)-glutathione + NADH + H+
-
-
-
-
?
3-ethoxy-2-hydroxybutyraldehyde + glutathione + NAD+
S-(3-ethoxy-2-hydroxybutyryl)-glutathione + NADH + H+
-
weak activity
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
-
ir
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
main enzymatic system responsible for the formaldehyde elimination
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzymatic degradation of formaldehyde seems to play an important role in resistance against formaldehyde
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzyme is involved in methanol metabolism
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzyme is involved in methanol metabolism
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
Dipodascus klebahnii
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
Dipodascus klebahnii
-
resistance to formaldehyde is attributed to detoxification by oxidation
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzymatic degradation of formaldehyde seems to play an important role in resistance against formaldehyde
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
inducible enzyme, at least one function of the enzyme in Gram-negative bacteria is to detoxify exogenous formaldehyde encountered in their environment
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzymatic degradation of formaldehyde seems to play an important role in resistance against formaldehyde
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
inducible enzyme, at least one function of the enzyme in Gram-negative bacteria is to detoxify exogenous formaldehyde encountered in their environment
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
r
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
r
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
-
r
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
at pH 8 the rate of the reverse reaction with S-formylglutathione and NADH is about the same as that of the forward reaction with formaldehyde, glutathione and NAD+. At pH 5.7 the rate of the reverse reaction with S-formylglutathione and NADH is 3.9times and with S-formylglutathione and NADPH 2.0times, that of the forward reaction rate with NAD+ at pH 8.0
-
?, r
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the enzyme activity in increased in livers from cancer patients independent of alcohol drinking or nondrinking, with no significant differences between primary and metastatic tumors
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzymatic degradation of formaldehyde seems to play an important role in resistance against formaldehyde
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
Kloeckera sp.
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
r
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
r
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
r
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzyme of the formaldehyde oxidation pathway via the linear sequence
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzyme of the formaldehyde oxidation pathway via the linear sequence
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
Methylophilus methanolovorus
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
principal enzyme for biological formaldehyde oxidation
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzyme of methanol dissimilation. When cells are grown on glucose, the enzyme is not detected during the exponential growth, but is formed in the late stationary phase without addition of methanol. Enzyme is synthesized during growth on sorbitol, glycerol, ribose and xylose
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
key enzyme in formaldehyde metabolism in microorganisms
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
key enzyme in formaldehyde metabolism in microorganisms
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
principal enzyme for biological formaldehyde oxidation
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
principal enzyme for biological formaldehyde oxidation
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
main enzymatic system responsible for the formaldehyde elimination
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
Protaminobacter candidus
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzymatic degradation of formaldehyde seems to play an important role in resistance against formaldehyde
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
r
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
r
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
r
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
main enzymatic system responsible for the formaldehyde elimination
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzyme is not essential but enhances the resistance against formaldehyde
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
resistance to formaldehyde is attributed to detoxification by oxidation
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzymatic degradation of formaldehyde seems to play an important role in resistance against formaldehyde
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
r
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
r
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
r
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
inducible enzyme
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzyme is found only in methanol-grown cells and is absent in cells grown on ethanol or glucose as carbon source
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
principal enzyme for biological formaldehyde oxidation
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
key enzyme of the dissimilatory pathway of the methanol metabolism
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the synthesis of the enzyme is induced by methanol and repressed by glucose
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
key step of the methanol catabolism in yeast
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
r
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
key step of the methanol catabolism in yeast
-
-
?
formaldehyde + glutathione + NADP+
S-formylglutathione + NADPH + H+
-
-
-
r
formaldehyde + glutathione + NADP+
S-formylglutathione + NADPH + H+
-
-
-
r
formaldehyde + glutathione + NADP+
S-formylglutathione + NADPH + H+
-
-
-
r
formaldehyde + glutathione + NADP+
S-formylglutathione + NADPH + H+
-
-
-
r
formaldehyde + S-hydroxymethyl glutathione + NAD+
?
-
-
-
-
?
formaldehyde + S-hydroxymethyl glutathione + NAD+
?
-
-
-
-
?
formaldehyde + S-hydroxymethyl glutathione + NAD+
?
-
-
-
-
?
formaldehyde + S-hydroxymethyl glutathione + NAD+
?
-
-
-
-
?
formaldehyde + S-hydroxymethyl glutathione + NAD+
?
-
-
-
-
?
formaldehyde + S-hydroxymethyl glutathione + NAD+
?
-
-
-
-
?
formaldehyde + S-hydroxymethyl glutathione + NAD+
?
-
-
-
-
?
glyoxal + glutathione + NAD+
S-oxoacetylglutathione + NADH
-
-
-
-
?
glyoxal + glutathione + NAD+
S-oxoacetylglutathione + NADH
-
weak activity
-
-
?
glyoxal + glutathione + NAD+
S-oxoacetylglutathione + NADH
-
35% of the activity with formaldehyde
-
-
?
glyoxal + glutathione + NAD+
S-oxoacetylglutathione + NADH
-
-
-
-
?
hydroxypyruvaldehyde + glutathione + NAD+
S-hydroxypyruvylglutathione + NADH
-
-
-
-
?
hydroxypyruvaldehyde + glutathione + NAD+
S-hydroxypyruvylglutathione + NADH
-
weak activity
-
-
?
methylglyoxal + glutathione + NAD+
S-pyruvylglutathione + NADH
-
-
-
-
?
methylglyoxal + glutathione + NAD+
S-pyruvylglutathione + NADH
-
-
-
-
?
methylglyoxal + glutathione + NAD+
S-pyruvylglutathione + NADH
-
85% of the activity with formaldehyde
-
-
?
methylglyoxal + glutathione + NAD+
S-pyruvylglutathione + NADH
-
-
-
-
?
methylglyoxal + glutathione + NAD+
S-pyruvylglutathione + NADH
-
-
-
-
?
methylglyoxal + glutathione + NAD+
S-pyruvylglutathione + NADH
-
90% of the activity with formaldehyde
-
-
?
methylglyoxal + glutathione + NAD+
S-pyruvylglutathione + NADH
-
-
-
-
?
methylglyoxal + glutathione + NAD+
S-pyruvylglutathione + NADH
-
-
-
-
?
methylglyoxal + glutathione + NAD+
S-pyruvylglutathione + NADH
-
-
-
-
?
methylglyoxal + glutathione + NAD+
S-pyruvylglutathione + NADH
-
-
-
-
?
methylglyoxal + glutathione + NAD+
S-pyruvylglutathione + NADH
-
-
-
-
?
methylglyoxal + glutathione + NAD+
S-pyruvylglutathione + NADH
-
-
-
-
?
methylglyoxal + glutathione + NAD+
S-pyruvylglutathione + NADH
-
89% of the activity with formaldehyde
-
-
?
methylglyoxal + glutathione + NAD+
S-pyruvylglutathione + NADH
-
89% of the activity with formaldehyde
-
-
?
octanol + glutathione + NAD+
?
-
-
-
-
?
octanol + glutathione + NAD+
?
-
octanol-1
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
essential role in formaldehyde detoxifcation
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
the enzyme plays an important role in the formaldehyde detoxification and reduction of the nitric oxide metabolite
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-formylglutathione + NADH
formaldehyde + glutathione + NAD+
-
-
-
r
S-formylglutathione + NADH
formaldehyde + glutathione + NAD+
-
-
-
r
S-formylglutathione + NADH
formaldehyde + glutathione + NAD+
-
-
-
r
S-formylglutathione + NADH
formaldehyde + glutathione + NAD+
-
-
-
r
S-formylglutathione + NADH
formaldehyde + glutathione + NAD+
-
-
-
r
S-formylglutathione + NADH
formaldehyde + glutathione + NAD+
-
-
-
r
S-formylglutathione + NADH
formaldehyde + glutathione + NAD+
-
-
-
r
S-formylglutathione + NADH
formaldehyde + glutathione + NAD+
-
-
-
r
S-formylglutathione + NADH
formaldehyde + glutathione + NAD+
-
-
-
r
S-formylglutathione + NADH
formaldehyde + glutathione + NAD+
-
-
-
r
S-formylglutathione + NADH
formaldehyde + glutathione + NAD+
-
-
-
r
S-formylglutathione + NADH
formaldehyde + glutathione + NAD+
-
-
-
r
S-formylglutathione + NADPH
formaldehyde + glutathione + NADP+
-
-
-
r
S-formylglutathione + NADPH
formaldehyde + glutathione + NADP+
-
-
-
r
S-hydroxymethylglutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
-
?
S-hydroxymethylglutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
-
?
S-hydroxymethylglutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
-
?
S-hydroxymethylglutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
-
r
S-nitrosoglutathione + NAD(P)H + H+
?
-
-
-
-
?
S-nitrosoglutathione + NAD(P)H + H+
?
-
NADPH-dependent activity is higher than NADH-dependent activity
-
-
?
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NADH
? + NAD+
-
-
-
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
-
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
-
-
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
-
-
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
-
-
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
-
-
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
-
-
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
a variety of products depending on cellular conditions, including glutathione disulfide, glutathione sulfinamide and hydroxylamine
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
a variety of products depending on cellular conditions, including glutathione disulfide, glutathione sulfinamide and hydroxylamine
-
?
S-nitrosoglutathione + NADH
GSH + NAD+ + NO
-
-
-
-
?
S-nitrosoglutathione + NADH
GSH + NAD+ + NO
-
the enzyme provides a defense mechanism against nitrosative stress, enzymatic pathway that modulates the bioactivity and toxicity of NO
-
-
?
S-nitrosoglutathione + NADH
GSH + NAD+ + NO
-
-
-
-
?
S-nitrosoglutathione + NADH
GSH + NAD+ + NO
-
-
-
-
?
S-nitrosoglutathione + NADH + H+
?
-
-
-
-
?
S-nitrosoglutathione + NADH + H+
?
-
-
-
-
?
S-nitrosoglutathione + NADH + H+
?
-
-
-
-
?
S-nitrosoglutathione + NADH + H+
?
-
-
-
-
?
S-nitrosoglutathione + NADH + H+
?
-
-
-
-
?
S-nitrosoglutathione + NADH + H+
?
-
-
-
?
S-nitrosoglutathione + NADH + H+
? + NAD+
-
-
-
?
S-nitrosoglutathione + NADH + H+
? + NAD+
-
-
-
?
S-nitrosoglutathione + NADH + H+
? + NAD+
-
-
-
-
?
S-nitrosoglutathione + NADH + H+
glutathione disulfide + hydroxylamine + NH4+ + NAD+
-
-
-
?
S-nitrosoglutathione + NADH + H+
glutathione disulfide + hydroxylamine + NH4+ + NAD+
-
-
-
?
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
S-amino-L-glutathione + NAD+ + ?
-
-
-
-
r
S-nitrosoglutathione + NADH + H+
S-amino-L-glutathione + NAD+ + ?
-
ADH3 can affect the transnitrosation equilibrium between S-nitrosoglutathione and S-nitrosated proteins, arguing for an important role in NO homeostasis
-
-
?
S-nitrosoglutathione + NADPH + H+
glutathione disulfide + hydroxylamine + NH4+ + NADP+
-
-
-
?
S-nitrosoglutathione + NADPH + H+
glutathione disulfide + hydroxylamine + NH4+ + NADP+
-
-
-
?
S-nitrosoglutathione + NADPH + H+
GSSG + ammonia + NADP+
-
-
-
ir
S-nitrosoglutathione + NADPH + H+
GSSG + ammonia + NADP+
-
-
-
ir
S-nitrosoglutathione + NADPH + H+
GSSG + ammonia + NADP+
-
-
-
ir
S-nitrosoglutathione + NADPH + H+
GSSG + ammonia + NADP+
-
-
-
-
ir
additional information
?
-
alcohol dehydrogenase 3, ADH3, acts as S-nitrosylglutathione reductase catalyzing the NADH-dependent reduction of S-nitrosoglutathione to GSSG and NH3, but also shows detoxification of formaldehyde catalyzing the formation of S-formylglutathione from formaldehyde and GSH
-
-
?
additional information
?
-
in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
-
-
-
additional information
?
-
plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant
-
-
-
additional information
?
-
enzyme additionally has aldehyde reductase activity, acting on formaldehyde, acetaldehyde, propionaldehyde with 2-20% of the activity with S-nitrosoglutathione
-
-
?
additional information
?
-
-
enzyme additionally has aldehyde reductase activity, acting on formaldehyde, acetaldehyde, propionaldehyde with 2-20% of the activity with S-nitrosoglutathione
-
-
?
additional information
?
-
enzyme additionally has aldehyde reductase activity, acting on formaldehyde, acetaldehyde, propionaldehyde with 2-20% of the activity with S-nitrosoglutathione
-
-
?
additional information
?
-
in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a cosubstrate in the reduction of GSNO
-
-
-
additional information
?
-
-
no substrate: glutathione disulfide
-
-
-
additional information
?
-
in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
-
-
-
additional information
?
-
plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant
-
-
-
additional information
?
-
in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
-
-
-
additional information
?
-
plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant
-
-
-
additional information
?
-
genes adhC and nmlRHI are required for defense against S-nitrosoglutathione in the organism, regulation of the adhC-estD operon, overview
-
-
?
additional information
?
-
-
genes adhC and nmlRHI are required for defense against S-nitrosoglutathione in the organism, regulation of the adhC-estD operon, overview
-
-
?
additional information
?
-
AdhC has NADH-dependent S-nitrosoglutathione reductase activity
-
-
?
additional information
?
-
-
AdhC has NADH-dependent S-nitrosoglutathione reductase activity
-
-
?
additional information
?
-
genes adhC and nmlRHI are required for defense against S-nitrosoglutathione in the organism, regulation of the adhC-estD operon, overview
-
-
?
additional information
?
-
AdhC has NADH-dependent S-nitrosoglutathione reductase activity
-
-
?
additional information
?
-
in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
-
-
-
additional information
?
-
plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant
-
-
-
additional information
?
-
-
the enzyme plays an important role in the metabolism of glutathione adducts such as S-(hydroxymethyl)glutathione and S-nitrosoglutathione
-
-
?
additional information
?
-
S-nitrosoglutathione (GSNO) binding to Lys188, Gly321, and Lys323. In the presence of glutathione (GSH), N-hydroxysulfenamido glutathione is converted to hydroxylamine and glutathione disulfide (GSSG)
-
-
-
additional information
?
-
in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
-
-
-
additional information
?
-
plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant. GSNO is reduced with 15-20times higher catalytic efficiency compared to the oxidation of HMGSH
-
-
-
additional information
?
-
in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
-
-
-
additional information
?
-
plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant
-
-
-
additional information
?
-
in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
-
-
-
additional information
?
-
plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant
-
-
-
additional information
?
-
key enzyme required for the catabolism of methanol as a carbon source and certain primary amines, such as methylamine as nitrogen sources in methylotrophic yeasts. The expression of FLDH1 is strictly regulated and can be controlled at two expression levels by manipulation of the growth conditions. The gene is strongly induced under methylotrophic growth conditions. Moderate expression is obtained under conditions in which a primary amine, e.g. methylamine is used as nitrogen source
-
-
?
additional information
?
-
-
enzyme detection in a coupled reaction of formaldehyde oxidation with formazan production from chromogenic agent NTB
-
-
?
additional information
?
-
-
enzyme detection in a coupled reaction of formaldehyde oxidation with formazan production from chromogenic agent NTB
-
-
?
additional information
?
-
FLD1 is involved in the detoxification of formaldehyde in methanol metabolism, and Fld1p coordinates the formaldehyde level in methanol-grown cells according to the methanol concentration on growth. FLD activity is mainly induced by methanol, and this induction is not completely repressed by glucose
-
-
?
additional information
?
-
-
FLD1 is involved in the detoxification of formaldehyde in methanol metabolism, and Fld1p coordinates the formaldehyde level in methanol-grown cells according to the methanol concentration on growth. FLD activity is mainly induced by methanol, and this induction is not completely repressed by glucose
-
-
?
additional information
?
-
-
in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
-
-
-
additional information
?
-
-
plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant. GSNO is reduced with 15-20times higher catalytic efficiency compared to the oxidation of HMGSH
-
-
-
additional information
?
-
in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
-
-
-
additional information
?
-
plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant
-
-
-
additional information
?
-
in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
-
-
-
additional information
?
-
plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant. GSNO is reduced with 15-20times higher catalytic efficiency compared to the oxidation of HMGSH
-
-
-
additional information
?
-
the reaction mechanism involved the oxidation of a hydroxyl group of S-(hydroxymethyl)glutathione, spontaneous adduct of formaldehyde and glutathione, to form S-formylglutathione. Substrate specificity with alcohols and omega-hydroxyfatty acids, overview
-
-
?
additional information
?
-
-
the reaction mechanism involved the oxidation of a hydroxyl group of S-(hydroxymethyl)glutathione, spontaneous adduct of formaldehyde and glutathione, to form S-formylglutathione. Substrate specificity with alcohols and omega-hydroxyfatty acids, overview
-
-
?
additional information
?
-
in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
-
-
-
additional information
?
-
plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant. GSNO is reduced with 15-20times higher catalytic efficiency compared to the oxidation of HMGSH
-
-
-
additional information
?
-
the reaction mechanism involved the oxidation of a hydroxyl group of S-(hydroxymethyl)glutathione, spontaneous adduct of formaldehyde and glutathione, to form S-formylglutathione. Substrate specificity with alcohols and omega-hydroxyfatty acids, overview
-
-
?
additional information
?
-
in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
-
-
-
additional information
?
-
plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant. GSNO is reduced with 15-20times higher catalytic efficiency compared to the oxidation of HMGSH
-
-
-
additional information
?
-
-
no activity for NO, S-nitrosocysteine, or S-nitrosohomocysteine
-
-
?
additional information
?
-
-
the enzyme may be involved in the detoxification of long-chain lipid peroxidation products
-
-
?
additional information
?
-
the enzyme is essential for growth on methanol
-
-
?
additional information
?
-
-
the enzyme is essential for growth on methanol
-
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
12-hydroxydodecanoic acid + glutathione + NAD+
S-(11-carboxy)undecanyl-glutathione + NADH + H+
-
best substrate for ADH3
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
formaldehyde + NAD+ + glutathione
S-formylglutathione + NADH
-
multifunctional enzyme, ADH3 constitutes a key enzyme in the detoxification of endogenous and exogenous formaldehyde, formaldehyde is released during intracellular metabolism of endogenous compounds or xenobiotics, expression of ADH3 might thus fulfill a protective role against DNA damage resulting from formaldehyde sources, ADH3 itself catalyzes oxidative reactions which produce NADH, most importantly the oxidation of formaldehyde
-
-
?
S-(hydroxymethyl)glutathione + NAD(P)+
S-formylglutathione + NAD(P)H + H+
-
multifunctional enzyme, large active site pocket of enzyme entails special substrate specificities: short-chain alcohols are poor substrates, while medium-chain alcohols and particularly the glutathione adducts S-hydroxymethylglutathioneand S-nitrosoglutathione are efficiently converted, universal presence and structural conservation imply that ADH3 performs essential housekeeping functions in living organisms
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
S-nitrosoglutathione + NADH
? + NAD+
S-nitrosoglutathione + NADH
GSH + NAD+ + NO
-
the enzyme provides a defense mechanism against nitrosative stress, enzymatic pathway that modulates the bioactivity and toxicity of NO
-
-
?
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
S-nitrosoglutathione + NADH + H+
GSSG + hydroxylamine + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
S-amino-L-glutathione + NAD+ + ?
-
ADH3 can affect the transnitrosation equilibrium between S-nitrosoglutathione and S-nitrosated proteins, arguing for an important role in NO homeostasis
-
-
?
S-nitrosoglutathione + NADPH + H+
GSSG + ammonia + NADP+
additional information
?
-
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
main enzymatic system responsible for the formaldehyde elimination
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzymatic degradation of formaldehyde seems to play an important role in resistance against formaldehyde
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzyme is involved in methanol metabolism
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzyme is involved in methanol metabolism
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
Dipodascus klebahnii
-
resistance to formaldehyde is attributed to detoxification by oxidation
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzymatic degradation of formaldehyde seems to play an important role in resistance against formaldehyde
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
inducible enzyme, at least one function of the enzyme in Gram-negative bacteria is to detoxify exogenous formaldehyde encountered in their environment
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzymatic degradation of formaldehyde seems to play an important role in resistance against formaldehyde
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
inducible enzyme, at least one function of the enzyme in Gram-negative bacteria is to detoxify exogenous formaldehyde encountered in their environment
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the enzyme activity in increased in livers from cancer patients independent of alcohol drinking or nondrinking, with no significant differences between primary and metastatic tumors
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzymatic degradation of formaldehyde seems to play an important role in resistance against formaldehyde
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzyme of the formaldehyde oxidation pathway via the linear sequence
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzyme of the formaldehyde oxidation pathway via the linear sequence
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
principal enzyme for biological formaldehyde oxidation
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzyme of methanol dissimilation. When cells are grown on glucose, the enzyme is not detected during the exponential growth, but is formed in the late stationary phase without addition of methanol. Enzyme is synthesized during growth on sorbitol, glycerol, ribose and xylose
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
key enzyme in formaldehyde metabolism in microorganisms
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
key enzyme in formaldehyde metabolism in microorganisms
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the true substrate is S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
principal enzyme for biological formaldehyde oxidation
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
principal enzyme for biological formaldehyde oxidation
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
main enzymatic system responsible for the formaldehyde elimination
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzymatic degradation of formaldehyde seems to play an important role in resistance against formaldehyde
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
main enzymatic system responsible for the formaldehyde elimination
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzyme is not essential but enhances the resistance against formaldehyde
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
resistance to formaldehyde is attributed to detoxification by oxidation
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzymatic degradation of formaldehyde seems to play an important role in resistance against formaldehyde
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
inducible enzyme
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
enzyme is found only in methanol-grown cells and is absent in cells grown on ethanol or glucose as carbon source
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
principal enzyme for biological formaldehyde oxidation
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
key enzyme of the dissimilatory pathway of the methanol metabolism
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
the synthesis of the enzyme is induced by methanol and repressed by glucose
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
key step of the methanol catabolism in yeast
-
-
?
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
-
key step of the methanol catabolism in yeast
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
essential role in formaldehyde detoxifcation
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
the enzyme plays an important role in the formaldehyde detoxification and reduction of the nitric oxide metabolite
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-(hydroxymethyl)glutathione + NAD+
S-formylglutathione + NADH + H+
-
-
-
?
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NAD(P)H + H+
GSSG + ammonia + NAD(P)+
-
-
-
ir
S-nitrosoglutathione + NADH
? + NAD+
-
-
-
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
-
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
-
-
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
-
-
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
-
-
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
-
-
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
-
-
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
a variety of products depending on cellular conditions, including glutathione disulfide, glutathione sulfinamide and hydroxylamine
-
?
S-nitrosoglutathione + NADH
? + NAD+
-
a variety of products depending on cellular conditions, including glutathione disulfide, glutathione sulfinamide and hydroxylamine
-
?
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADH + H+
GSSG + ammonia + NAD+
-
-
-
ir
S-nitrosoglutathione + NADPH + H+
GSSG + ammonia + NADP+
-
-
-
ir
S-nitrosoglutathione + NADPH + H+
GSSG + ammonia + NADP+
-
-
-
ir
S-nitrosoglutathione + NADPH + H+
GSSG + ammonia + NADP+
-
-
-
ir
S-nitrosoglutathione + NADPH + H+
GSSG + ammonia + NADP+
-
-
-
-
ir
additional information
?
-
alcohol dehydrogenase 3, ADH3, acts as S-nitrosylglutathione reductase catalyzing the NADH-dependent reduction of S-nitrosoglutathione to GSSG and NH3, but also shows detoxification of formaldehyde catalyzing the formation of S-formylglutathione from formaldehyde and GSH
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additional information
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in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
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additional information
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in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a cosubstrate in the reduction of GSNO
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additional information
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in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
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additional information
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in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
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additional information
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genes adhC and nmlRHI are required for defense against S-nitrosoglutathione in the organism, regulation of the adhC-estD operon, overview
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additional information
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genes adhC and nmlRHI are required for defense against S-nitrosoglutathione in the organism, regulation of the adhC-estD operon, overview
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additional information
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genes adhC and nmlRHI are required for defense against S-nitrosoglutathione in the organism, regulation of the adhC-estD operon, overview
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additional information
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in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
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additional information
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the enzyme plays an important role in the metabolism of glutathione adducts such as S-(hydroxymethyl)glutathione and S-nitrosoglutathione
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additional information
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in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
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additional information
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in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
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additional information
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in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
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additional information
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key enzyme required for the catabolism of methanol as a carbon source and certain primary amines, such as methylamine as nitrogen sources in methylotrophic yeasts. The expression of FLDH1 is strictly regulated and can be controlled at two expression levels by manipulation of the growth conditions. The gene is strongly induced under methylotrophic growth conditions. Moderate expression is obtained under conditions in which a primary amine, e.g. methylamine is used as nitrogen source
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additional information
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FLD1 is involved in the detoxification of formaldehyde in methanol metabolism, and Fld1p coordinates the formaldehyde level in methanol-grown cells according to the methanol concentration on growth. FLD activity is mainly induced by methanol, and this induction is not completely repressed by glucose
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additional information
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FLD1 is involved in the detoxification of formaldehyde in methanol metabolism, and Fld1p coordinates the formaldehyde level in methanol-grown cells according to the methanol concentration on growth. FLD activity is mainly induced by methanol, and this induction is not completely repressed by glucose
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additional information
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in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
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additional information
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in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
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additional information
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in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
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additional information
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in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
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additional information
?
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in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO
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additional information
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the enzyme may be involved in the detoxification of long-chain lipid peroxidation products
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additional information
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the enzyme is essential for growth on methanol
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additional information
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the enzyme is essential for growth on methanol
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evolution
the enzyme belongs to the large alcohol dehydrogenase superfamily, namely to the class III ADHs
evolution
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GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR belongs to the class III alcohol dehydrogenase family
evolution
GSNOR expression and activity during development of Solanum spp. genotypes
evolution
GSNOR expression and activity during development of Solanum spp. genotypes
evolution
GSNOR expression and activity during development of Solanum spp. genotypes
evolution
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GSNOR is a member of class III alcohol dehydrogenase family
evolution
GSNOR is a member of class III alcohol dehydrogenase family
evolution
GSNOR is a member of class III alcohol dehydrogenase family
evolution
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GSNOR is a member of class III alcohol dehydrogenase family
evolution
GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1)
evolution
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GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins
evolution
GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins
evolution
GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins
evolution
GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins
evolution
GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins
evolution
GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins
evolution
GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins
evolution
GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins
evolution
GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins
evolution
GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins
evolution
GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins
evolution
GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins
evolution
S-nitrosoglutathione reductase (GSNOR) is highly conserved enzyme amongst eukaryotes and prokaryotes. It is a member of the class III alcohol dehydrogenase family
evolution
S-nitrosoglutathione reductase (GSNOR) is highly conserved enzyme amongst eukaryotes and prokaryotes. It is a member of the class III alcohol dehydrogenase family
evolution
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the enzyme belongs to the large alcohol dehydrogenase superfamily, namely to the class III ADHs
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malfunction
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mesenchymal stem cells deficient in GSNOR exhibit markedly diminished capacity for vasculogenesis in an in vitro Matrigel tubeforming assay and in vivo relative to wild-type cells. This decrease is associated with downregulation of the PDGF receptor alpha in GSNOR-/- mesenchymal stem cells, a receptor essential for VEGF-A action in the cells. GSNOR-/- mesenchymal stem cells have a deficient capacity for endothelial differentiation due to downregulation of PDGFRalpha related to NO/GSNOR imbalance, overview
malfunction
mutation of AtGSNOR1 modulates the level of cellular S-nitrosylglutathione formation and turnover, which appears to regulate multiple forms of plant disease resistance. GSNOR gene knockout mutant par2 is resistant to the herbicide paraquat, which acts by inducing the production of superoxide and hydrogen peroxide
malfunction
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overexpression of the fdh in the central nervous system significantly increases GSNOR activity and induces visual pattern memory defects of Drosophila melanogaster. Overexpression of the fdh in the fan-shaped body induces memory defect, while overexpression in the mushroom body does not. The visual pattern memory defect can be rescued by co-expression with exogenous cGMP-dependent protein kinase
malfunction
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S-nitrosothiols content and nitric oxide emission in Arabidopsis thaliana cell suspension cultures of wild-type and GSNOR overexpressing or antisense transgenic lines, grown under optimal conditions and under nutritional stress, overview. Overexpressing cells have the lowest S-nitrosothiols and nitric oxide levels and antisense cells the highest, hile under stress, this pattern is reversed. mitochondrial changes and phenotypes, overview
malfunction
silencing GSNOR decreases the herbivory-induced accumulation of jasmonic acid and ethylene, two important phytohormones regulating plant defence levels, without compromising the activity of two mitogen-activated protein kinases, salicylic acid-induced protein kinase and wound-induced protein kinase
malfunction
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a fast increase in S-nitrosothiol content and a reduction of the leaf photosynthesis ratio are a result of suppressed GSNOR activity with specific inhibitors
malfunction
a fast increase in S-nitrosothiol content and a reduction of the leaf photosynthesis ratio are a result of suppressed GSNOR activity with specific inhibitors
malfunction
a fast increase in S-nitrosothiol content and a reduction of the leaf photosynthesis ratio are a result of suppressed GSNOR activity with specific inhibitors
malfunction
a potential role of GSNOR in plant resistance to herbivory Manduca sexta is examined in coyote tobacco (Nicotiana attenuata) plants using a virus-induced silencing of GSNOR. GSNOR-silenced plants are more susceptible to herbivore attack and decreased the herbivore-induced accumulation of phytohormones jasmonic acid (JA) and ethylene and activity of trypsin proteinase inhibitors
malfunction
Arabidopsis thaliana plants overexpressing the GSNOR gene exhibit increased nitrate reductase (NR) activity, conversely, GSNOR mutant plants show a significant decrease in NR activity. GSNOR enzymatic activity, but not gene expression, is inhibited by the nitrogen assimilatory pathway via post-transcriptional S-nitrosation, preventing any scavenging of GSNO. Enzymatic activity of GSNOR is essential for the acclimation of Arabidopsis thaliana plants to high temperature, since HOT5 mutants, plants with defect GSNOR gene, are more sensitive to high temperature as a consequence of disturbed homeostasis of S-nitrosothiols and NO-derived ROS signaling pathways. Enzyme mutant Nox1 is an NO overproducing plant with higher levels of L-arginine and L-citrulline, while mutant Gsnor1-3 is a plant with reduced GSNOR activity with higher levels of NO, S-nitrosothiols, and nitrate. Gsnor1-3 mutant Arabidopsis thaliana plants with a high S-nitrosothiols level show an increased selenite tolerance. high NO level, due to the reduced GSNOR activity, increases sensitivity under mild stress conditions, while it supports tolerance under severe stress conditions. Gsnor1-3 mutant plants with a high S-nitrosothiols level show an increased selenite tolerance
malfunction
control female hearts exhibit enhanced functional recovery and decreased infarct size vs. control males. GSNO-R inhibition reverses this sex disparity, significantly reducing injury in male hearts, and exacerbating injury in females. Similar results are obtained with male and female GSNO-R-/- hearts using ex vivo and in vivo models of I/R injury. Assessment of SNO levels using SNO-resin assisted capture reveals an increase in total SNO levels with GSNO-R inhibition in males, whereas total SNO levels remain unchanged in females. While GSNO-R inhibition significantly increases SNO at the cardioprotective Cys39 residue of NADH dehydrogenase subunit 3 in males, SNO-ND3 levels are surprisingly reduced in N6022-treated female hearts. Since GSNO-R also acts as a formaldehyde dehydrogenase, post-ischemic formaldehyde levels are examined, they are nearly 2fold higher in N6022-treated female hearts compared to non-treated hearts. The mitochondrial aldehyde dehydrogenase 2 activator, Alda-1, rescues the phenotype in GSNO-R-/- female hearts, significantly reducing infarct size. Male GSNO-R-/- mice weigh significantly less than male wild-type mice. Male GSNO-R-/- hearts show a significant reduction in infarct size compared to wild-type. GSNO-R inhibition increases post-ischemic free formaldehyde levels in female hearts, and mitochondrial aldehyde dehydrogenase 2 activation reduces I/R injury in female GSNO-R-/- hearts. But formaldehyde does not compete with SNO for the modification of common cysteine residues
malfunction
depletion of GSNOR function impacts tomato (Solanum lycopersicum. L) fruit development. Thus, reduction of GSNOR expression through RNAi modulated both fruit formation and yield, establishing another function for GSNOR. Further, depletion of Solanum lycopersicum GSNOR (SlGSNOR) additionally impacted a number of other developmental processes, including seed development, which also has not been previously linked with GSNOR activity. Depletion of GSNOR function does not influence root development in tomato. Reduction of GSNOR transcript abundance compromises plant immunity. Overexpression of SlGSNOR promotes resistance to bacterial pathogens, such as Pseudomonas syringae pv. tomato DC3000 (PstDC3000)
malfunction
GSNOR knockdown significantly impairs blastocyst formation and quality and markedly induces the increase in protein S-nitrosylation. Notably, GSNOR knockdown-induced overproduction of S-nitrosylation caused mitochondrial dysfunction, including mitochondrial membrane potential depolarization, mitochondria-derived reactive oxygen species (ROS) increase and ATP deficiency. GSNOR knockdown-induced total mitochondrial amount increase, but the ratio of active mitochondria reduction, suggesting that the damaged mitochondria are accumulated and mitochondrial clearance is inhibited. In addition, damaged mitochondria produce more ROS, and cause DNA damage and apoptosis. Supplementation with pan-NOS inhibitor Nomega-nitro-L-arginine methyl ester hydrochloride (L-NAME) reverses the increase in S-nitrosylation, accumulation of damaged mitochondria, and oxidative stress-induced cell death. Autophagy is downregulated after GSNOR knock-down, but reversed by L-NAME treatment
malfunction
GSNOR knockout mutated plants often display a stunted growth phenotype in all structures, and exhibit a pre-induced protective effect against oxidative stressors, as well as an improved immune response associated with NO accumulation in roots. GSNOR knockout strains display reduced primary root growth under high iron conditions, but relatively no change is observed in wild-type seedlings. Plant systems reversibly inhibit their GSNOR activity in response to oxidative radicals
malfunction
GSNOR knockout mutated plants often display a stunted growth phenotype in all structures, and exhibit a pre-induced protective effect against oxidative stressors, as well as an improved immune response associated with NO accumulation in roots. The action of increasing NO levels and GSNOR1 inhibition is often coupled with increased ROSs associated with plant immune response. Plant systems reversibly inhibit their GSNOR activity in response to oxidative radicals
malfunction
GSNOR overexpression improves root tolerance to NH4+. The root growth in two OsGSNOR knockout lines (Osgsnor-1 and Osgsnor-2) is significantly more sensitive to NH4+ than in wild-type. Loss of GSNOR further induces NO accumulation, increases SNO1/SOS4 activity, and reduces K+ levels in root tissue, enhancing root growth sensitivity to NH4+
malfunction
GSNOR overexpression in tomato plant has little effect on growth and development, whereas GSNOR downregulated plants are significantly smaller, suggesting a role for NO and S-nitrosothiol signaling
malfunction
identification of 334 endogenously S-nitrosylated proteins with 425 S-nitrosylated sites site-specific nitrosoproteomic approach from the wild-type and GSNOR-knockdown tomato plants under both control and sodic alkaline stress conditions, detailed overview. These S-nitrosylated proteins are involved in a wide range of various metabolic, cellular and catalytic processes
malfunction
in leaves of Lactuca saligna during interactions with biotrophic mildews, Bremia lactucae (lettuce downy mildew), Golovinomyces cichoracearum (lettuce powdery mildew) and non-pathogen Pseudoidium neolycopersici (tomato powdery mildew) during 168 h post inoculation (hpi), the GSNOR expression is increased both in the early phase at 6 hpi and later phase at 72 hpi, with increased GSNOR-mediated decrease of S-nitrosothiols
malfunction
in leaves of Lactuca sativa during interactions with biotrophic mildews, Bremia lactucae (lettuce downy mildew), Golovinomyces cichoracearum (lettuce powdery mildew) and non-pathogen Pseudoidium neolycopersici (tomato powdery mildew) during 168 h post inoculation (hpi), the GSNOR expression is highly increased both in the early phase at 6 hpi and later phase at 72 hpi, with increased GSNOR-mediated decrease of S-nitrosothiols
malfunction
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in leaves of Lactuca serriola during interactions with biotrophic mildews, Bremia lactucae (lettuce downy mildew), Golovinomyces cichoracearum (lettuce powdery mildew) and non-pathogen Pseudoidium neolycopersici (tomato powdery mildew) during 168 h post inoculation (hpi), the GSNOR expression is increased both in the early phase at 6 hpi and later phase at 72 hpi, with increased GSNOR-mediated decrease of S-nitrosothiols
malfunction
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in leaves of Lactuca virosa during interactions with biotrophic mildews, Bremia lactucae (lettuce downy mildew), Golovinomyces cichoracearum (lettuce powdery mildew) and non-pathogen Pseudoidium neolycopersici (tomato powdery mildew) during 168 h post inoculation (hpi), the GSNOR expression is increased both in the early phase at 6 hpi and later phase at 72 hpi, with increased GSNOR-mediated decrease of S-nitrosothiols
malfunction
increased expression of the reductase in preterm myometrium is associated with decreased total protein S-nitrosation. Global protein S-nitrosation is also diminished in spontaneously in labor preterm (sPTL). Blockade of S-nitrosoglutathione reductase relaxes sPTL tissue. Addition of NO donor to the actin motility assay attenuates force. Failure of soluble guanylyl cyclase (sGC) activation to mediate relaxation in sPTL tissues, together with the ability of NO to relax labor at term (TL), but not sPTL myometrium, suggests a unique pathway for NO-mediated relaxation in myometrium. Blockade of GSNOR activity relaxes term non-laboring (TNL) myometrium. GSNOR inhibition affects force, and force reduction may be consistent with S-nitrosations lowering the threshold for contractions until term
malfunction
increased NO content is involved in NH4+ inhibition of root growth. GSNOR overexpression improves root tolerance to NH4+, phenotypes, overview. Loss of GSNOR further induces NO accumulation, increases SNO1/SOS4 activity, and reduces K+ levels in root tissue, enhancing root growth sensitivity to NH4+. NO contributes to NH4+-inhibited K+ absorption in Arabidopsis at least partly via enhanced SNO1/SOS4 activity. The NH4+-induced GSNOR protein accumulation is abolished in the VTC1- (vitamin C1) defective mutant vtc1-1, which is hypersensititive to NH4+ toxicity. GSNOR overexpression enhances vtc1-1 root tolerance to NH4+
malfunction
overexpression alleviates chlorosis under Fe-deficiency conditions. GSNOR overexpression positively regulates the Fe distribution from root to shoot, which might result from the transcriptional regulation of genes involved in Fe metabolism. Overexpression of GSNOR maintains redox homeostasis and protects chloroplasts from Fe deficiency-related damage, resulting in a greater photosynthetic capacity. As a nitric oxide regulator, GSNOR's overexpression decreases the excessive accumulation of nitric oxide and S-nitrosothiols during the Fe deficiency, and maintains the homeostases of reactive oxygen species and reactive nitrogen species. Moreover, GSNOR overexpression, probably at the level of genes and proteins, along with protein S-nitrosylation, promotes Fe uptake and regulates the shoot/root Fe ratio under Fe-deficiency conditions. The overexpression of GSNOR alleviates the Fe-deficiency-induced oxidative stress
malfunction
overexpression of SoGSNOR in tobacco increases the germination rate of transgenic seeds, compared to the wild-type under nitrate stress. Higher photosynthetic rate, transpiration rate, stomatal conductance, water use efficiency and expression level of some stress-related genes are detected in the transgenic seedlings compared to wild-type under nitrate stress. The transgenic tobacco seedlings have lower malondialdehyde content, reactive oxygen species (ROS) fluorescence, and higher activities and transcript level of superoxide dismutase, catalase, peroxidase under nitrate stress. SoGSNOR transgenic tobacco plants have lower nitrate reductase activity and protein level, higher GSNOR and non-symbiotic class 1 hemoglobin (nsHb) protein level than the wild-type plants, leading to lower NO accumulation and SNOs contents under nitrate stress. Overexpression of SoGSNOR increases nitrate stress tolerance of tobacco by regulating ROS and RNS metabolism
malfunction
oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. In tomato, the expression of GSNOR is significantly affected by alkaline stress. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
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oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
pharmacological inhibition of S-nitrosoglutathione reductase reduces cardiac damage induced by ischemia-reperfusion
malfunction
suppression of S-nitrosoglutathione reductase (GSNOR) promotes axillary buds outgrowth via inhibiting the expression of flavin monooxygenase (FZY) in both apical and axillary buds. Meanwhile, AUX1 and PIN1 are downregulated in apical buds but upregulated in axillary buds in GSNOR-suppressed plants. Thus, reduced indoleacetic acid (IAA) accumulation is shown in both apical buds and axillary buds of GSNOR-suppressed plants. A decreased ratio of auxin:cytokinin is observed in axillary buds of GSNOR-suppressed plants, leading to buds dormancy breaking. GSNOR plays a positive role in regulating FZY expression and IAA level in apical buds. Notably, levels of IAA in axillary buds show similar patterns with that in apical buds, but an inhibition of FZY transcript in axillary buds is observed by both overexpression and suppression of GSNOR. Silencing FZY results in auxin biosynthesis inhibition and axillary buds outgrowth. Inhibitory effects on FZY expression and IAA accumulation lead to highly branched phenotype in tomato plants
malfunction
the disease incidence and lesion diameter of peach fruits inoculated with pathogen Monilinia fructicola are significantly suppressed by NO and GSNOR inhibitor (N6022), and the inhibitory effect of GSONR inhibitor on Monilinia fructicola is better than that of NO solution treatment. Compared with the control, NO and GSNOR inhibitor obviously enhance the activity of glutathione reductase (GR)
malfunction
the dysregulation of GSNOR expression is implicated in several organ system pathologies including respiratory, cardiovascular, hematologic, and neurologic, making GSNOR a primary target for pharmacological intervention
malfunction
the gsnor-ko plants contain elevated amount of low and high molecular weight S-nitrosothiols (SNO) indicating that GSNOR activity controls the level of both GSNO and indirectly protein-SNOs. GSNOR deficiency has been shown to cause pleiotropic plant growth defects, impaired plant disease responses, heat sensitivity, and resistance to cell death. Oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR
malfunction
water stress, a problem for plant growth and productivity, in Lotus japonicus leads to both oxidative and nitrosative stress. Among others, cellular NO and S-nitrosothiol content are increased, GSNOR activity is reduced, and protein tyrosine nitration is stimulated
malfunction
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increased NO content is involved in NH4+ inhibition of root growth. GSNOR overexpression improves root tolerance to NH4+, phenotypes, overview. Loss of GSNOR further induces NO accumulation, increases SNO1/SOS4 activity, and reduces K+ levels in root tissue, enhancing root growth sensitivity to NH4+. NO contributes to NH4+-inhibited K+ absorption in Arabidopsis at least partly via enhanced SNO1/SOS4 activity. The NH4+-induced GSNOR protein accumulation is abolished in the VTC1- (vitamin C1) defective mutant vtc1-1, which is hypersensititive to NH4+ toxicity. GSNOR overexpression enhances vtc1-1 root tolerance to NH4+
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malfunction
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S-nitrosothiols content and nitric oxide emission in Arabidopsis thaliana cell suspension cultures of wild-type and GSNOR overexpressing or antisense transgenic lines, grown under optimal conditions and under nutritional stress, overview. Overexpressing cells have the lowest S-nitrosothiols and nitric oxide levels and antisense cells the highest, hile under stress, this pattern is reversed. mitochondrial changes and phenotypes, overview
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malfunction
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control female hearts exhibit enhanced functional recovery and decreased infarct size vs. control males. GSNO-R inhibition reverses this sex disparity, significantly reducing injury in male hearts, and exacerbating injury in females. Similar results are obtained with male and female GSNO-R-/- hearts using ex vivo and in vivo models of I/R injury. Assessment of SNO levels using SNO-resin assisted capture reveals an increase in total SNO levels with GSNO-R inhibition in males, whereas total SNO levels remain unchanged in females. While GSNO-R inhibition significantly increases SNO at the cardioprotective Cys39 residue of NADH dehydrogenase subunit 3 in males, SNO-ND3 levels are surprisingly reduced in N6022-treated female hearts. Since GSNO-R also acts as a formaldehyde dehydrogenase, post-ischemic formaldehyde levels are examined, they are nearly 2fold higher in N6022-treated female hearts compared to non-treated hearts. The mitochondrial aldehyde dehydrogenase 2 activator, Alda-1, rescues the phenotype in GSNO-R-/- female hearts, significantly reducing infarct size. Male GSNO-R-/- mice weigh significantly less than male wild-type mice. Male GSNO-R-/- hearts show a significant reduction in infarct size compared to wild-type. GSNO-R inhibition increases post-ischemic free formaldehyde levels in female hearts, and mitochondrial aldehyde dehydrogenase 2 activation reduces I/R injury in female GSNO-R-/- hearts. But formaldehyde does not compete with SNO for the modification of common cysteine residues
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malfunction
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pharmacological inhibition of S-nitrosoglutathione reductase reduces cardiac damage induced by ischemia-reperfusion
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metabolism
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metabolism and signaling function of nitric oxide and S-nitrosoglutathione in plant peroxisomes, overview
metabolism
S-nitrosylglutathione metabolism in plant cells and its regulation by GSNO reductase, overview
metabolism
along with its more stable NO donor, S-nitroso-glutathione (GSNO), formed by NO non-enzymatically in the presence of glutathione (GSH), NO is a redox-active molecule capable of mediating target protein cysteine thiols through the post translational modification, S-nitrosation. S-nitroso-glutathione reductase (GSNOR) thereby acts as a mediator to pathways regulated by NO due to its activity in the irreversible reduction of GSNO to oxidized glutathione (GSSG) and ammonia. GSNOR is thought to be pleiotropic and often acts by mediating the cellular environment in response to stress conditions. Under optimal conditions its activity leads to growth by transcriptional upregulation of the nitrate transporter, NRT2.1, and through its interaction with phytohormones like auxin and strigolactones associated with root development. GSNOR is required in times of iron toxicity. Mechanism for control of the nitrogen assimilation pathway. GSNOR activity is thought to increase NRT2.1 and nitrate reductase (NR) function thereby leading to eventual increases in NO levels, which are ultimately thought to have an inhibitory effect on GSNOR
metabolism
along with its more stable NO donor, S-nitroso-glutathione (GSNO), formed by NO non-enzymatically in the presence of glutathione (GSH), NO is a redox-active molecule capable of mediating target protein cysteine thiols through the post translational modification, S-nitrosation. S-nitroso-glutathione reductase (GSNOR) thereby acts as a mediator to pathways regulated by NO due to its activity in the irreversible reduction of GSNO to oxidized glutathione (GSSG) and ammonia. GSNOR is thought to be pleiotropic and often acts by mediating the cellular environment in response to stress conditions. Under optimal conditions its activity leads to growth by transcriptional upregulation of the nitrate transporter, NRT2.1, and through its interaction with phytohormones like auxin and strigolactones associated with root development. GSNOR is required in times of iron toxicity. Mechanism for control of the nitrogen assimilation pathway. GSNOR activity is thought to increase NRT2.1 and nitrate reductase (NR) function thereby leading to eventual increases in NO levels, which are ultimately thought to have an inhibitory effect on GSNOR
metabolism
role of S-nitrosoglutathione reductase in the regulation of reactive nitrogen species metabolism in Solanum spp., modeling, overview
metabolism
role of S-nitrosoglutathione reductase in the regulation of reactive nitrogen species metabolism in Solanum spp., modeling, overview
metabolism
role of S-nitrosoglutathione reductase in the regulation of reactive nitrogen species metabolism in Solanum spp., modeling, overview
metabolism
S-(hydroxymethyl)glutathione dehydrogenase is involved in the S-nitrosothiol metabolism and GSNO degrading
metabolism
site-specific nitrosoproteomic analysis, GSNOR is the key scavenger for sodic alkaline stress-induced S-nitrosylation
physiological function
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ADH3 plays a minor role in hepatic alcohol metabolism
physiological function
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Arabidopsis GSNOR1/HOT5 gene regulates salicylic acid signaling and thermotolerance by modulating the intracellular S-nitrosothiol level. Arabidopsis paraquat resistant2-1 (par2-1) mutant shows an anti-cell death phenotype. GSNOR1/HOT5/PAR2 plays an important role in regulating cell death in plant cells through modulating intracellular NO level
physiological function
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CBR1 may be involved in regulation of tissue levels of S-nitrosoglutathione, but inhibits ca. 30% of the NADPH-dependent activity
physiological function
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formaldehyde toxicity in Adh3 null mutant mice is significantly increased relative to that in wild-type mice. Adh3-deficient mice demonstrate significantly decreased levels of all-trans-retinoic acid in serum, providing evidence for the involvement of ADH3 in retinoic acid formation in vivo
physiological function
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GSNOR is able to regulate the level of S-nitrosoglutathione and indirectly the NO content and its availability
physiological function
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GSNOR is an important regulator of airway S-nitrosothiol content and airways hyperresponsiveness in human asthma
physiological function
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GSNOR limits nitric oxide-mediated suppression of NF-kappaB and activation of soluble guanylyl cyclase
physiological function
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importance of ADH3 in formaldehyde resistance
physiological function
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importance of ADH3 in formaldehyde resistance. Mutants with modified ADH3 expression seem incapable of detecting intracellular changes in the GSH pool
physiological function
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importance of GSNOR-regulated NO homeostasis to abiotic stress and plant development. GSNOR affects intracellular NO/nitrosation levels
physiological function
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important ADH3 roles in embryonic development
physiological function
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important ADH3 roles in embryonic development
physiological function
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important ADH3 roles in embryonic development
physiological function
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NtrA is a bifunctional enzyme that exhibits nitroreductase and S-nitrosoglutathione reductase activity. Even though the presence of NtrA contributes to the activation of nitrofurans, in the absence of these antibiotics NtrA acts as a defense system that allows the decomposition of endogenously formed S-nitrosoglutathione, which occurs when Staphylococcus aureus is exposed to nitrosative stress, thus avoiding the harmful effects caused by transnitrosylation reactions. Inactivation of the putative nitroreductase SA0UHSC_00833 increases the sensitivity to S-nitrosoglutathione and augments its resistance to nitrofurans. Expression of NtrA from the pMK4 plasmid restores the wild-type phenotype
physiological function
the enzyme GFD is bifunctional. In addition to the glutathione-dependent formaldehyde dehydrogenase activity, it also functions as an effective S-nitrosoglutathione reductase presumably to safeguard against nitrosative stress
physiological function
GSNOR activity is necessary for normal development and fertility under optimal growth conditions. The GSNOR gene is regulated by wounding and salicylic acid
physiological function
GSNOR is required for methyl jasmonate-induced accumulation of defence-related secondary metabolites (TPI, caffeoylputrescine, and diterpene glycosides) but is not needed for the transcriptional regulation of JAZ3 (jasmonate ZIM-domain 3) and TD (threonine deaminase), indicating that GSNOR mediates certain but not all jasmonate-inducible responses
physiological function
in plants, GSNOR plays an important role in biotic and abiotic stress responses. S-nitrosylglutathione serves as a nitric oxide reservoir locally or possibly as NO donor in distant cells and tissues. NO and NO-related molecules such as S-nitrosothiols play a central role in the regulation of normal plant physiological processes and host defence. The key enzyme participates in the cellular homeostasis of S-NOs and in the metabolism of reactive nitrogen species
physiological function
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S-nitrosoglutathione reductase catalyzes its decomposition and protein tyrosine nitration
physiological function
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S-nitrosoglutathione reductase is a denitrosylase that regulates S-nitrosylation
physiological function
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the enzyme controls the nitric oxide metabolism, which plays a crucial role in visual pattern memory in Drosophila melanogaster. The role of fdh in learning and memory is independent of development and is neuron-specific
physiological function
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the enzyme has an important role in the metabolism of S-nitrosothiols and in the modulation of nitric oxide-mediated processes, post-transcriptional regulation, overview
physiological function
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biofilm formation remains unaffected under nitrosative stress in Vibrio cholerae
physiological function
enzyme deletion mutants are lethal in formaldehyde containing medium, sensitive to exogenous NO and exhibit a higher level of S-nitrosothiols than wild type. The mutants show severe reduction of conidiation and appressoria turgor pressure, as well as significantly attenuated the virulence on rice cultivar CO-39. The virulence of deletion mutants on wounded rice leaf is not affected. Deletion mutants exhibit a lower infection rate, and growth of infectious hyphae of the mutants is retarded not only in primary infected cells but also in expansion from cell to cell. Deletion mutants display hypersensitivity to different oxidants, reduced activities of superoxide dismutases and peroxidases, and lower glutathione content in cells, compared with the wild type
physiological function
heterologous expression in HEK 293T cells results in higher viability and less apoptosis under nitrosative stress induced by S-nitrosoglutathione
physiological function
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inactivation of the FrxA-encoding gene results in a strain more sensitive to S-nitrosoglutathione. FrxA contributes to the proliferation of Helicobacter pylori in macrophages and FrxA supports the virulence of the pathogen upon mouse infection
physiological function
the FldA gene is able to functionally complement a Saccharomyces cerevisiae strain lacking the gene for S-hydroxymethylglutathione dehydrogenase. The expression renders the Sacchamormyces cerevisiae mutant strain tolerant to exogenous formaldehyde. Although the parent strain is unable to degrade even low concentrations of formaldehyde, the recombinant strain is able to degrade 4 mM formaldehyde within 30 h
physiological function
glutathione-dependent formaldehyde dehydrogenase (GFD) from Taiwanofungus camphorata plays important roles in formaldehyde detoxification and antioxidation. The enzyme is bifunctional. In addition to the GFD activity, it also functions as an effective S-nitrosoglutathione reductase (GSNOR) against nitrosative stress. Formaldehyde detoxification involves the conversion of formaldehyde to formate, which consists of three reactions: The first reaction is a spontaneous condensation reaction between formaldehyde and glutathione producing S-hydroxymethylglutathione (HMGSH). The second reaction, catalyzed by enzyme GFD, is the oxidation of HMGSH to form S-formylglutathione. In the third reaction, catalyzed by S-formylglutathione hydrolase (FGH), formate is formed and glutathione regenerated
physiological function
enzyme GSNOR is a nitric oxide regulator and is involved in responses to iron deficiency, GSNOR-regulated RNS homeostasis under Fe-deficiency conditions, overview. Ferric-chelate reductase activity is regulated by GSNOR
physiological function
induction of S-nitrosoglutathione reductase protects root growth from ammonium toxicity by regulating potassium homeostasis in Arabidopsis thaliana. GSNOR negatively regulates ammonium-mediated NO accumulation and K+ imbalance, Arabidopsis thaliana GSNOR is a master regulator of the intracellular NO level
physiological function
key role of GSNOR and modulations of reactive nitrogen species (RNS) during plant development under normal conditions pointing to their involvement in molecular mechanisms of tomato responses to biotrophic pathogens on local and systemic levels
physiological function
key role of GSNOR and modulations of reactive nitrogen species (RNS) during plant development under normal conditions pointing to their involvement in molecular mechanisms of tomato responses to biotrophic pathogens on local and systemic levels
physiological function
key role of GSNOR and modulations of reactive nitrogen species (RNS) during plant development under normal conditions pointing to their involvement in molecular mechanisms of tomato responses to biotrophic pathogens on local and systemic levels
physiological function
nitric oxide (NO) is emerging as a key signalling molecule in plants. The chief mechanism for the transfer of NO bioactivity is thought to be S-nitrosylation, the addition of an NO moiety to a protein cysteine thiol to form an S-nitrosothiol (SNO). The enzyme S-nitrosoglutathione reductase (GSNOR) indirectly controls the total levels of cellular S-nitrosylation, by depleting S-nitrosoglutathione (GSNO), the major cellular NO donor. SlGSNOR regulates seed devlopment, fruit production, and flower development, overview
physiological function
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nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling
physiological function
protein S-nitros(yl)ation (SNO) has been implicated as an essential mediator of nitric oxide-dependent cardioprotection. Compared to males, female hearts exhibit higher baseline levels of protein SNO and associated with this, reduced susceptibility to myocardial ischemia-reperfusion (I/R) injury. Female hearts also exhibit enhanced S-nitrosoglutathione reductase (GSNO-R) activity, which would typically favor decreased SNO levels as GSNO-R mediates SNO catabolism. Since female hearts exhibit higher SNO levels, GSNO-R seems to be an essential component of sex-dependent cardioprotection in females. GSNO-R is a critical sex-dependent mediator of myocardial protein SNO and formaldehyde levels. GSNO-R activity is significantly enhanced in female hearts at baseline vs. males
physiological function
S-nitrosoglutathione (GSNO) reductase (GSNOR) is the enzymatic regulator of endogenous S-nitrosoglutathione availability. GSNO alters actin-myosin motility. Effect of GSNO on protein S-nitrosation in human myometrium, overview
physiological function
S-nitrosoglutathione reductase (GSNOR) is an enzyme involved in the metabolism of S-nitrosothiols by producing denitrosylation, thus limiting the cardioprotective effect of NO. Cardioprotective effects of nitric oxide (NO) have been described through S-nitrosylation of several important proteins in the mitochondria of the cardiomyocyte. GSNOR plays a role in normal cardiac function, affecting vascular tone and cardiac contractility
physiological function
S-nitrosoglutathione reductase (GSNOR) is capable of the NADH-dependent reduction of GSNO to glutathione disulfide (GSSG), the oxidized form of GSH, and ammonium (NH3). It has been originally identified in plants as a glutathione-dependent formaldehyde dehydrogenase (FALDH), and a member of the class III alcohol dehydrogenase family, where the primary substrate is hemithioacetal S-hydroxymethylglutathione (HMGSH), which is formed in an oxidizing environment through the favorable reaction of formaldehyde and GSH, using a catalytic zinc, and in the presence of the coenzyme NAD+. The redox-active enzyme acts in the homeostasis of S-nitrosothiols (SNOs) and is capable of regulating many cellular processes in that manner. Role of GSNOR in root development, overview. Although it is expressed within many plant tissues, GSNOR is thought to be localized in the phloem and xylem parenchyma cells of the vasculature, capable of regulating NO levels throughout the plant. GSNOR activity is related to NO production. Auxin is an important hormone capable of mediating cellular growth in concert with GSNOR. Auxin signalling is specifically relevant when considering the growth of root structures in response to GSNO levels, where a mechanism has been identified to regulate TIR1, a nuclear F-box protein and the auxin receptor. At increased GSNO levels, and thereby reduced GSNOR activity, S-nitrosation of TIR1 receptor is thought to increase its affinity for auxin and in turn increase transcription of target proteins. GSNOR may play a role in controlling strigolactones (SL) induced primary root elongation
physiological function
S-nitrosoglutathione reductase (GSNOR) is capable of the NADH-dependent reduction of GSNO to glutathione disulfide (GSSG), the oxidized form of GSH, and ammonium (NH3). It has been originally identified in plants as a glutathione-dependent formaldehyde dehydrogenase (FALDH), and a member of the class III alcohol dehydrogenase family, where the primary substrate is hemithioacetal S-hydroxymethylglutathione (HMGSH), which is formed in an oxidizing environment through the favorable reaction of formaldehyde and GSH, using a catalytic zinc, and in the presence of the coenzyme NAD+. The redox-active enzyme acts in the homeostasis of S-nitrosothiols (SNOs) and is capable of regulating many cellular processes in that manner. Role of GSNOR in root development, overview. Although it is expressed within many plant tissues, GSNOR is thought to be localized in the phloem and xylem parenchyma cells of the vasculature, capable of regulating NO levels throughout the plant. GSNOR activity is related to NO production. Auxin is an important hormone capable of mediating cellular growth in concert with GSNOR. Auxin signalling is specifically relevant when considering the growth of root structures in response to GSNO levels, where a mechanism has been identified to regulate TIR1, a nuclear F-box protein and the auxin receptor. At increased GSNO levels, and thereby reduced GSNOR activity, S-nitrosation of TIR1 receptor is thought to increase its ax0enity for auxin and in turn increase transcription of target proteins. GSNOR may play a role in controlling strigolactones (SL) induced primary root elongation
physiological function
S-nitrosoglutathione reductase (GSNOR) is the central enzyme for regulating protein S-nitrosylation. GSNOR is a NAD+-dependent aldehyde dehydrogenase. It can also catalyze the NADH-coupled reduction of S-nitrosoglutathione (GSNO) to N-hydroxysulfenamido glutathione. In the presence of glutathione (GSH), N-hydroxysulfenamido glutathione is converted to hydroxylamine and glutathione disulfide (GSSG)
physiological function
S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Important role of GSNOR and S-nitrosation in adaptation of Chlamydomonas reinhardtii to salt stress
physiological function
S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress
physiological function
S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress
physiological function
S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress
physiological function
S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress
physiological function
S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. Regulation of GSNOR activity through S-nitrosation of conserved cysteines is observed in Arabidopsis thaliana plants. GSNOR activity might be regulated by high levels of NO donors. Changes in GSNOR levels have an influence on the activities of mitochondrial complex I, external NADH dehydrogenase, alternative oxidase and uncoupling protein. GSNOR modulates the activity of the mitochondrial respiratory chain through controlling NO/SNO homeostasis under physiological conditions and under nutritional stress. Regulatory mechanisms of GSNOR in protein denitrosation on the intersection of signaling pathways of ROSs and RNSs. GSNOR is involved in plant responses to cold and heat stress
physiological function
S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress. NO and GSNO, as S-nitrosating agents, and GSNOR are found to be involved in the programmed cell death (PCD) induced by heat shock or H2O2 in tobacco (Nicotiana tabacum) bright yellow-2 cells
physiological function
S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress
physiological function
S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR mediates some jasmonate-dependent responses, e.g., the accumulation of defense secondary metabolites. GSNOR is involved in plant responses to cold and heat stress
physiological function
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S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR modulates NO-induced nitrosative stress in rice plants grown under aluminum stress, which leads to accumulation of both ROSs and RNSs
physiological function
S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR modulates NO-induced nitrosative stress in rice plants grown under aluminum stress, which leads to accumulation of both ROSs and RNSs
physiological function
S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR modulates NO-induced nitrosative stress in rice plants grown under aluminum stress, which leads to accumulation of both ROSs and RNSs
physiological function
S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR modulates NO-induced nitrosative stress in rice plants grown under aluminum stress, which leads to accumulation of both ROSs and RNSs
physiological function
S-nitrosoglutathione reductase (GSNOR) negatively regulates NO homeostasis. GSNOR-mediated changes of NO and auxin affect cytokinin biosynthesis, transport, and signaling. suppression of GSNOR decreased the transcripts of AUX1 and PIN1 in apical buds, but increased the transcripts of AUX1 and PIN1 in axillary buds. GSNOR-controlled NO plays important roles in controlling axillary buds outgrowth via altering the homeostasis and signaling of auxin and cytokinin in tomato plants
physiological function
S-nitrosoglutathione reductase maintains mitochondrial homeostasis by promoting clearance of damaged mitochondria in porcine preimplantation embryos. GSNOR maintains mitochondrial homeostasis by promoting autophagy and the clearing of damaged mitochondria in porcine preimplantation embryos
physiological function
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S-nitrosylation belongs to principal signalling pathways of nitric oxide in plant development and stress responses. Protein S-nitrosylation is regulated by S-nitrosoglutathione reductase (GSNOR) as a key catabolic enzyme of S-nitrosoglutathione (GSNO), the major intracellular S-nitrosothiol. GSNOR metabolizes S-nitrosoglutathione irreversibly to glutathione disulphide (GSSG) and ammonia (NH3)
physiological function
S-nitrosylation belongs to principal signalling pathways of nitric oxide in plant development and stress responses. Protein S-nitrosylation is regulated by S-nitrosoglutathione reductase (GSNOR) as a key catabolic enzyme of S-nitrosoglutathione (GSNO), the major intracellular S-nitrosothiol. GSNOR metabolizes S-nitrosoglutathione irreversibly to glutathione disulphide (GSSG) and ammonia (NH3)
physiological function
S-nitrosylation belongs to principal signalling pathways of nitric oxide in plant development and stress responses. Protein S-nitrosylation is regulated by S-nitrosoglutathione reductase (GSNOR) as a key catabolic enzyme of S-nitrosoglutathione (GSNO), the major intracellular S-nitrosothiol. GSNOR metabolizes S-nitrosoglutathione irreversibly to glutathione disulphide (GSSG) and ammonia (NH3)
physiological function
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S-nitrosylation belongs to principal signalling pathways of nitric oxide in plant development and stress responses. Protein S-nitrosylation is regulated by S-nitrosoglutathione reductase (GSNOR) as a key catabolic enzyme of S-nitrosoglutathione (GSNO), the major intracellular S-nitrosothiol. GSNOR metabolizes S-nitrosoglutathione irreversibly to glutathione disulphide (GSSG) and ammonia (NH3)
physiological function
S-nitrosylation, regulated by S-nitrosoglutathione reductase (GSNOR), is considered as an important route for nitric oxide (NO)-modulated stress tolerance in plants. Proteins involving in NO homeostasis control, signaling of Ca2+, ethylene and MAPK, reactive oxygen species (ROS) scavenging, osmotic regulation, as well as energy support pathway are identified and selected as the key and sensitive targets that are regulated by GSNOR-modulated S-nitrosylation in response to sodic alkaline stress. GSNOR is actively involved in the regulation of sodic alkaline stress tolerance by S-nitrosylation. Phenotypes, overview
physiological function
S-nitrosylation, the addition of nitric oxide (NO) moiety to a reactive cysteine thiol, to form an S-nitrosothiol (SNO), is a prototypic redox-based post-translational modification. S-nitrosoglutathione reductase (GSNOR) is the major regulator of total cellular SNO levels in plants. It plays a role in excess nitrate stress
physiological function
the GSNOR-like gene, OsGSNOR, is required for NH4+ tolerance in rice. The OsGSNOR contributes to both K+ homeostasis and root growth tolerance to NH4+ in rice
physiological function
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enzyme deletion mutants are lethal in formaldehyde containing medium, sensitive to exogenous NO and exhibit a higher level of S-nitrosothiols than wild type. The mutants show severe reduction of conidiation and appressoria turgor pressure, as well as significantly attenuated the virulence on rice cultivar CO-39. The virulence of deletion mutants on wounded rice leaf is not affected. Deletion mutants exhibit a lower infection rate, and growth of infectious hyphae of the mutants is retarded not only in primary infected cells but also in expansion from cell to cell. Deletion mutants display hypersensitivity to different oxidants, reduced activities of superoxide dismutases and peroxidases, and lower glutathione content in cells, compared with the wild type
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physiological function
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induction of S-nitrosoglutathione reductase protects root growth from ammonium toxicity by regulating potassium homeostasis in Arabidopsis thaliana. GSNOR negatively regulates ammonium-mediated NO accumulation and K+ imbalance, Arabidopsis thaliana GSNOR is a master regulator of the intracellular NO level
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physiological function
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the enzyme has an important role in the metabolism of S-nitrosothiols and in the modulation of nitric oxide-mediated processes, post-transcriptional regulation, overview
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physiological function
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protein S-nitros(yl)ation (SNO) has been implicated as an essential mediator of nitric oxide-dependent cardioprotection. Compared to males, female hearts exhibit higher baseline levels of protein SNO and associated with this, reduced susceptibility to myocardial ischemia-reperfusion (I/R) injury. Female hearts also exhibit enhanced S-nitrosoglutathione reductase (GSNO-R) activity, which would typically favor decreased SNO levels as GSNO-R mediates SNO catabolism. Since female hearts exhibit higher SNO levels, GSNO-R seems to be an essential component of sex-dependent cardioprotection in females. GSNO-R is a critical sex-dependent mediator of myocardial protein SNO and formaldehyde levels. GSNO-R activity is significantly enhanced in female hearts at baseline vs. males
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physiological function
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the FldA gene is able to functionally complement a Saccharomyces cerevisiae strain lacking the gene for S-hydroxymethylglutathione dehydrogenase. The expression renders the Sacchamormyces cerevisiae mutant strain tolerant to exogenous formaldehyde. Although the parent strain is unable to degrade even low concentrations of formaldehyde, the recombinant strain is able to degrade 4 mM formaldehyde within 30 h
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physiological function
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S-nitrosoglutathione reductase (GSNOR) is an enzyme involved in the metabolism of S-nitrosothiols by producing denitrosylation, thus limiting the cardioprotective effect of NO. Cardioprotective effects of nitric oxide (NO) have been described through S-nitrosylation of several important proteins in the mitochondria of the cardiomyocyte. GSNOR plays a role in normal cardiac function, affecting vascular tone and cardiac contractility
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physiological function
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in plants, GSNOR plays an important role in biotic and abiotic stress responses. S-nitrosylglutathione serves as a nitric oxide reservoir locally or possibly as NO donor in distant cells and tissues. NO and NO-related molecules such as S-nitrosothiols play a central role in the regulation of normal plant physiological processes and host defence. The key enzyme participates in the cellular homeostasis of S-NOs and in the metabolism of reactive nitrogen species
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additional information
structure-function analysis, overview
additional information
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structure-function analysis, overview
additional information
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cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues
additional information
cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues. But the Arabidopsis GSNOR has neither intermolecular nor intramolecular redox-sensitive disulfide bridges. Cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site where Cys47 and Cys177 are involved in coordinating the catalytic Zn2+. Especially these two cysteine residues are sensitive to oxidation, whereas Cys271 localized in the NAD+ cofactor binding site is resistant to H2O2 induced oxidation
additional information
location of the GSNO allosteric domain comprising the residues Asn185, Lys188, Gly321, and Lys323 in the vicinity of the structural Zn2+-binding site, docking and molecular dynamics simulations utilizing the GSNOR crystal structure (PDB ID 3QJ5)as the template structure, HDX-MS data, overview
additional information
Solanum lycopersicum SlGSNOR structure in coordination with NAD+, the active sites on the homodimer coordinate the zinc ion, a possible point of regulation in the presence of oxidative species
additional information
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structure-function analysis, overview
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