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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
?
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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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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
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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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enzyme detection in a coupled reaction of formaldehyde oxidation with formazan production from chromogenic agent NTB
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enzyme detection in a coupled reaction of formaldehyde oxidation with formazan production from chromogenic agent NTB
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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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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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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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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
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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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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
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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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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
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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
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additional information
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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
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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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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
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additional information
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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
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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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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
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no activity for NO, S-nitrosocysteine, or S-nitrosohomocysteine
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the enzyme may be involved in the detoxification of long-chain lipid peroxidation products
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the enzyme is essential for growth on methanol
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the enzyme is essential for growth on methanol
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