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2-naphthaldehyde + NAD+ + H2O
2-naphthoate + NADH + H+
low dehydrogenase activity
-
-
?
2-naphthaldehyde + NADP+ + H2O
2-naphthoate + NADPH + H+
low dehydrogenase activity
-
-
?
2-oxoglutarate semialdehyde + NAD+ + H2O
2-oxoglutarate + NADH + H+
2-oxoglutarate semialdehyde + NADP+ + H2O
2-oxoglutarate + NADPH + H+
3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH + 2 H+
-
-
-
-
?
3-hydroxy-benzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
-
good substrate
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + 2 H+
-
-
-
-
?
3-sulfopropanal + NAD(P)+ + H2O
3-sulfopropanoate + NAD(P)H + 2 H+
-
-
-
?
4-chloro-benzaldehyde + NAD+ + H2O
4-chlorobenzoate + NADH + H+
-
good substrate
-
-
?
4-chlorobenzaldehyde + NAD+ + H2O
4-chlorobenzoate + NADH + 2 H+
-
-
-
-
?
acetaldehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
benzaldehyde + NADP+ + H2O
benzoate + NADPH + 2 H+
-
mandelate pathway
-
-
ir
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
beta-hydroxysuccinic semialdehyde + NADP+ + H2O
beta-hydroxysuccinate + NADPH + H+
-
-
-
?
cyclohexanal + NAD+ + H2O
? + NADH + 2 H+
-
-
-
-
?
cyclohexanal + NAD+ + H2O
cyclohexanecarboxylic acid + NADH + H+
-
good substrate
-
-
?
decanal + NAD+ + H2O
decanoate + NADH + H+
low dehydrogenase activity
-
-
?
decanal + NADP+ + H2O
decanoate + NADPH + H+
low dehydrogenase activity
-
-
?
heptanal + NAD+ + H2O
heptanoate + NADH + H+
-
good substrate
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + 2 H+
-
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
good substrate
-
-
?
malonic semialdehyde + NADP+ + H2O
malonate + NADPH + H+
-
hydrolyzed at 8.7% the rate of succinate semialdehyde
-
?
octanal + NAD+ + H2O
octanoate + NADH + H+
-
good substrate
-
-
?
pentanal + NAD+ + H2O
pentanoate + NADH + 2 H+
-
-
-
-
?
pentanal + NAD+ + H2O
pentanoate + NADH + H+
-
good substrate
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
succinic semialdehyde + NAD+ + H2O
succinate + NADH + H+
succinic semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
-
?
additional information
?
-
2-oxoglutarate semialdehyde + NAD+ + H2O
2-oxoglutarate + NADH + H+
-
-
-
-
?
2-oxoglutarate semialdehyde + NAD+ + H2O
2-oxoglutarate + NADH + H+
-
-
-
-
?
2-oxoglutarate semialdehyde + NADP+ + H2O
2-oxoglutarate + NADPH + H+
-
-
-
-
?
2-oxoglutarate semialdehyde + NADP+ + H2O
2-oxoglutarate + NADPH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
mandelate pathway
-
-
ir
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
-
weak reaction
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
-
weaker reaction compared to NAD+
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
-
weaker reaction compared to NAD+
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
r
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
r
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
r
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
r
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
r
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
r
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
r
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
NADP+ is the preferred cofactor
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
NADP+ is the preferred cofactor
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
NADP+ is the preferred cofactor
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
NADP+ is the preferred cofactor
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
NADP+ is the preferred cofactor
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
r
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
r
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
degradation of 3,4-dihydroxyphenylacetate in Arthrobacter sp.
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
degradation of 3,4-dihydroxyphenylacetate in Arthrobacter sp.
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
involved in the degradation of gamma-aminobutyrate
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
implicated in 4-hydroxyphenylacetic acid and gamma-aminobutyric acid catabolism
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
implicated in 4-hydroxyphenylacetic acid and gamma-aminobutyric acid catabolism
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
implicated in 4-hydroxyphenylacetic acid and gamma-aminobutyric acid catabolism
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
ir
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
at 9% of the rate with NAD+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
pathway for utilization of 4-aminobutyric acid as nitrogen source for Saccharomyces cerevisiae
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
-
?
succinic semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
succinic semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
additional information
?
-
protein cce4228 shows similar catalytic efficiency towards succinate semialdehyde (SSA) at saturated concentration of NAD+ or NADP+
-
-
-
additional information
?
-
protein cce4228 shows similar catalytic efficiency towards succinate semialdehyde (SSA) at saturated concentration of NAD+ or NADP+
-
-
-
additional information
?
-
-
only the aldehyde forms and not the gem-diol forms of the specific substrate succinic semialdehyde , of selected aldehyde substrates, and of the inhibitor 3-tolualdehyde bind to the enzyme. Residue cysteine311 is crucial for their discrimination
-
-
?
additional information
?
-
-
almost no activity with DL-glyceraldehyde, DL-glyceraldehyde 3-phosphate, and glycoaldehyde
-
-
?
additional information
?
-
-
other aldehydes, such as formaldehyde, acetaldehyde and glutaraldehyde, are very poor substrates
-
-
?
additional information
?
-
the enzyme is also active with D-glyceraldehyde 3-phosphate (Ga3P), cf. EC 1.2.1.90. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. Preference for NADP+ when SSA is the substrate
-
-
-
additional information
?
-
-
the enzyme is also active with D-glyceraldehyde 3-phosphate (Ga3P), cf. EC 1.2.1.90. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. Preference for NADP+ when SSA is the substrate
-
-
-
additional information
?
-
the enzyme is also active with D-glyceraldehyde 3-phosphate (Ga3P), cf. EC 1.2.1.90. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. Preference for NADP+ when SSA is the substrate
-
-
-
additional information
?
-
the enzyme is also active with D-glyceraldehyde 3-phosphate (Ga3P), cf. EC 1.2.1.90. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. Preference for NADP+ when SSA is the substrate
-
-
-
additional information
?
-
the enzyme is also active with D-glyceraldehyde 3-phosphate (Ga3P), cf. EC 1.2.1.90. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. Preference for NADP+ when SSA is the substrate
-
-
-
additional information
?
-
the enzyme is also active with D-glyceraldehyde 3-phosphate (Ga3P), cf. EC 1.2.1.90. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. Preference for NADP+ when SSA is the substrate
-
-
-
additional information
?
-
-
no activity with 2-chlorobenzaldehyde, 3-chlorobenzaldehyde, and acetaldehyde
-
-
?
additional information
?
-
-
no activity is observed with 2-chlorobenzaldehyde
-
-
?
additional information
?
-
-
the 3- and 4-chloro substituents as well as the 3-hydroxy substituent are all electron withdrawing. All these compounds show a reduction in reaction velocity from that of the unsubstituted benzaldehyde
-
-
?
additional information
?
-
-
almost no activity with D,L-glyceraldehyde, D,L-glyceraldehyde-3-phosphate, and D,L-glycolaldehyde
-
-
?
additional information
?
-
the enzyme shows no detectable activity with hexanal or benzaldehyde
-
-
?
additional information
?
-
-
the enzyme shows no detectable activity with hexanal or benzaldehyde
-
-
?
additional information
?
-
neither propionaldehyde nor phthalaldehyde seves as substrate
-
-
?
additional information
?
-
-
neither propionaldehyde nor phthalaldehyde seves as substrate
-
-
?
additional information
?
-
neither propionaldehyde nor phthalaldehyde seves as substrate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-naphthaldehyde + NAD+ + H2O
2-naphthoate + NADH + H+
low dehydrogenase activity
-
-
?
2-naphthaldehyde + NADP+ + H2O
2-naphthoate + NADPH + H+
low dehydrogenase activity
-
-
?
2-oxoglutarate semialdehyde + NAD+ + H2O
2-oxoglutarate + NADH + H+
-
-
-
-
?
2-oxoglutarate semialdehyde + NADP+ + H2O
2-oxoglutarate + NADPH + H+
-
-
-
-
?
3-sulfopropanal + NAD(P)+ + H2O
3-sulfopropanoate + NAD(P)H + 2 H+
-
-
-
?
acetaldehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
benzaldehyde + NADP+ + H2O
benzoate + NADPH + 2 H+
-
mandelate pathway
-
-
ir
decanal + NAD+ + H2O
decanoate + NADH + H+
low dehydrogenase activity
-
-
?
decanal + NADP+ + H2O
decanoate + NADPH + H+
low dehydrogenase activity
-
-
?
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
succinic semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
additional information
?
-
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
mandelate pathway
-
-
ir
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
r
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
r
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
r
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
r
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
degradation of 3,4-dihydroxyphenylacetate in Arthrobacter sp.
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
degradation of 3,4-dihydroxyphenylacetate in Arthrobacter sp.
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
involved in the degradation of gamma-aminobutyrate
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
implicated in 4-hydroxyphenylacetic acid and gamma-aminobutyric acid catabolism
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
implicated in 4-hydroxyphenylacetic acid and gamma-aminobutyric acid catabolism
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
implicated in 4-hydroxyphenylacetic acid and gamma-aminobutyric acid catabolism
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
pathway for utilization of 4-aminobutyric acid as nitrogen source for Saccharomyces cerevisiae
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
-
?
additional information
?
-
-
almost no activity with DL-glyceraldehyde, DL-glyceraldehyde 3-phosphate, and glycoaldehyde
-
-
?
additional information
?
-
-
other aldehydes, such as formaldehyde, acetaldehyde and glutaraldehyde, are very poor substrates
-
-
?
additional information
?
-
the enzyme shows no detectable activity with hexanal or benzaldehyde
-
-
?
additional information
?
-
-
the enzyme shows no detectable activity with hexanal or benzaldehyde
-
-
?
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0.1 - 0.3
2-oxoglutarate semialdehyde
0.041
3-sulfopropanal
Km apparent value
0.0069 - 0.035
benzaldehyde
0.002 - 20.5
succinate semialdehyde
0.0011 - 0.03
Succinic semialdehyde
additional information
additional information
-
0.1
2-oxoglutarate semialdehyde
-
with NAD+ as cosubstrate, at pH 6.5 and 70°C
0.2
2-oxoglutarate semialdehyde
-
with NADP+ as cosubstrate, at pH 6.5 and 70°C
0.3
2-oxoglutarate semialdehyde
-
in 0.1 M HEPES/KOH (pH 6.5), at 70°C
0.0069
benzaldehyde
-
in the presence of NADP+, at 25°C and pH 8.5
0.0071
benzaldehyde
-
in the presence of NAD+, at 25°C and pH 8.5
0.011
benzaldehyde
-
recombinant wild type enzyme, in the presence of NADP+, TAPS buffer, at pH 8.5, at 30°C
0.011
benzaldehyde
-
His-tagged BADH, cosubstrate NADP+
0.013
benzaldehyde
-
native wild type enzyme, in the presence of NADP+, TAPS buffer, at pH 8.5, at 30°C
0.013
benzaldehyde
-
wild-type BADH, cosubstrate NADP+
0.033
benzaldehyde
-
native wild type enzyme, in the presence of NAD+, TAPS buffer, at pH 8.5, at 30°C
0.033
benzaldehyde
-
wild-type BADH, cosubstrate NAD+
0.035
benzaldehyde
-
recombinant wild type enzyme, in the presence of NAD+, TAPS buffer, at pH 8.5, at 30°C
0.035
benzaldehyde
-
His-tagged BADH, cosubstrate NAD+
0.0092
NAD+
-
in the presence of 10 mM Mg2+, at pH 7.5 and 37°C
0.033
NAD+
-
pH 7.8, 30°C
0.043
NAD+
wild-type, pH 8.0, 37°C
0.043
NAD+
wild type enzyme, in 50 mM HEPES (pH 8.0), at 37°C
0.107
NAD+
-
pH 8.0, 30°C
0.111
NAD+
-
recombinant wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C
0.111
NAD+
-
His-tagged BADH, cosubstrate benzaldehyde
0.134
NAD+
-
native wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C
0.134
NAD+
-
wild-type BADH, cosubstrate benzaldehyde
0.15
NAD+
mutant enzyme N193A, in 50 mM HEPES (pH 8.0), at 37°C
0.15
NAD+
mutant N193A, pH 8.0, 37°C
0.21
NAD+
-
pH and temperature not specified in the publication
0.21
NAD+
pH not specified in the publication, 30°C
0.23
NAD+
Km apparent value
0.23
NAD+
recombinant His6-tagged enzyme, pH 7.0, 30°C
0.48
NAD+
wild-type, pH 8.0, 37°C
0.51
NAD+
pH 9.0, 25°C, recombinant mutant S157E
0.997
NAD+
-
in the presence of benzaldehyde, at 25°C and pH 8.5
1.12
NAD+
pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde
1.5
NAD+
pH 9.0, 25°C, recombinant mutant K154A
1.7
NAD+
pH 9.0, 25°C, recombinant wild-type enzyme
9.1
NAD+
-
in 0.1 M HEPES/KOH (pH 6.5), at 70°C
9.4
NAD+
-
mitochondria of non-synaptic origin
10
NAD+
mutant enzyme K160A, in 50 mM HEPES (pH 8.0), at 37°C
10
NAD+
mutant K160A , pH 8.0, 37°C
11
NAD+
mutant enzyme K160E, in 50 mM HEPES (pH 8.0), at 37°C
11
NAD+
mutant K160E , pH 8.0, 37°C
11.1
NAD+
-
at pH 6.5 and 70°C
0.004
NADP+
pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde
0.01
NADP+
-
at pH 6.5 and 70°C
0.034
NADP+
pH 9.0, 25°C, recombinant wild-type enzyme
0.0613
NADP+
-
in the absence of Mg2+, at pH 7.5 and 37°C
0.1
NADP+
recombinant His6-tagged enzyme, pH 7.0, 30°C
0.154
NADP+
-
pH 7.8, 30°C
0.22
NADP+
-
native wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C
0.22
NADP+
-
wild-type BADH, cosubstrate benzaldehyde
0.287
NADP+
-
recombinant wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C
0.287
NADP+
-
His-tagged BADH, cosubstrate benzaldehyde
0.35
NADP+
Km apparent value
0.39
NADP+
-
pH and temperature not specified in the publication
0.39
NADP+
pH not specified in the publication, 30°C
0.482
NADP+
wild type enzyme, in 50 mM HEPES (pH 8.0), at 37°C
1.1
NADP+
pH 9.0, 25°C, recombinant mutant S157E
2.4
NADP+
mutant enzyme N193A, in 50 mM HEPES (pH 8.0), at 37°C
2.4
NADP+
mutant N193A, pH 8.0, 37°C
6.1
NADP+
pH 9.0, 25°C, recombinant mutant v
6.14
NADP+
-
in the presence of benzaldehyde, at 25°C and pH 8.5
26
NADP+
mutant enzyme K160A, in 50 mM HEPES (pH 8.0), at 37°C
26
NADP+
mutant K160A , pH 8.0, 37°C
27
NADP+
mutant enzyme K160E, in 50 mM HEPES (pH 8.0), at 37°C
27
NADP+
mutant K160E , pH 8.0, 37°C
0.002
succinate semialdehyde
pH 8.0, 60°C, cosubstrate: NAD+
0.0028
succinate semialdehyde
pH 9.0, 25°C, recombinant mutant S157E, with NAD+
0.0029
succinate semialdehyde
pH 8.0, 60°C, cosubstrate: NADP+
0.003
succinate semialdehyde
-
with NADP+ as cosubstrate, in the presence of 10 mM Mg2+, at pH 7.5 and 37°C
0.003
succinate semialdehyde
pH 8.5, 30°C, recombinant enzyme, with NADP+
0.003
succinate semialdehyde
pH 9.0, 25°C, recombinant mutant S157E, with NADP+
0.004
succinate semialdehyde
pH 9.0, 25°C, recombinant wild-type enzyme, with NAD+
0.007
succinate semialdehyde
pH 8.5, 30°C, recombinant enzyme, with NAD+
0.0073
succinate semialdehyde
-
pH 8.0, 30°C
0.008
succinate semialdehyde
pH 9.0, 25°C, recombinant wild-type enzyme, with NADP+
0.0133
succinate semialdehyde
-
with NADP+ as cosubstrate, in the absence of Mg2+, at pH 7.5 and 37°C
0.017
succinate semialdehyde
-
-
0.02
succinate semialdehyde
pH 9.0, 25°C, recombinant mutant K154A, with NAD+
0.02
succinate semialdehyde
pH 9.0, 25°C, recombinant mutant K154A, with NADP+
0.022
succinate semialdehyde
mutant enzyme R428A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.022
succinate semialdehyde
mutant R428A , cofactor NAD+, pH 8.0, 37°C
0.027
succinate semialdehyde
wild type enzyme, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.027
succinate semialdehyde
wild-type, cofactor NAD+, pH 8.0, 37°C
0.04
succinate semialdehyde
-
-
0.047
succinate semialdehyde
wild type enzyme, with NADP+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.047
succinate semialdehyde
wild-type, cofactor NADP+, pH 8.0, 37°C
0.054
succinate semialdehyde
-
pH 7.8, 30°C
0.12
succinate semialdehyde
mutant enzyme F138A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.12
succinate semialdehyde
mutant F138A , cofactor NAD+, pH 8.0, 37°C
0.14
succinate semialdehyde
mutant enzyme E442A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.14
succinate semialdehyde
mutant E442A, cofactor NAD+, pH 8.0, 37°C
0.16 - 0.18
succinate semialdehyde
-
either with NAD+ or with NADP+
0.22
succinate semialdehyde
mutant enzyme S425A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.22
succinate semialdehyde
mutant S425A , cofactor NAD+, pH 8.0, 37°C
0.23
succinate semialdehyde
mutant enzyme D426A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.23
succinate semialdehyde
mutant D426A , cofactor NAD+, pH 8.0, 37°C
0.77
succinate semialdehyde
mutant enzyme W141A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.77
succinate semialdehyde
mutant W141A , cofactor NAD+, pH 8.0, 37°C
1.06
succinate semialdehyde
-
-
1.4
succinate semialdehyde
-
synaptosomes
1.5
succinate semialdehyde
-
mitochondria of non-synaptic origin
2.49
succinate semialdehyde
mutant enzyme R145A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
2.49
succinate semialdehyde
mutant R145A , cofactor NAD+, pH 8.0, 37°C
2.6
succinate semialdehyde
mutant enzyme K92A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
2.6
succinate semialdehyde
mutant K92A, cofactor NAD+, pH 8.0, 37°C
10.36
succinate semialdehyde
cofactor NAD+, pH not specified in the publication, 30°C
10.36
succinate semialdehyde
-
pH and temperature not specified in the publication, in presence of NAD+
20.5
succinate semialdehyde
cofactor NADP+, pH not specified in the publication, 30°C
20.5
succinate semialdehyde
-
pH and temperature not specified in the publication, in presence of NADP+
0.0011
Succinic semialdehyde
-
with NAD+ as cosubstrate, at pH 6.5 and 70°C
0.004
Succinic semialdehyde
-
with NADP+ as cosubstrate, at pH 6.5 and 70°C
0.03
Succinic semialdehyde
-
in 0.1 M HEPES/KOH (pH 6.5), at 70°C
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics, kinetic analysis
-
additional information
additional information
-
Michaelis-Menten kinetics, kinetic analysis
-
additional information
additional information
Michaelis-Menten kinetics, steady-state kinetics of cce4228 wild-type and mutants enzymes
-
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7.1 - 27.3
2-oxoglutarate semialdehyde
0.1 - 164
succinate semialdehyde
16.8 - 22.6
Succinic semialdehyde
7.1
2-oxoglutarate semialdehyde
-
in 0.1 M HEPES/KOH (pH 6.5), at 70°C
21.2
2-oxoglutarate semialdehyde
-
with NADP+ as cosubstrate, at pH 6.5 and 70°C
27.3
2-oxoglutarate semialdehyde
-
with NAD+ as cosubstrate, at pH 6.5 and 70°C
6.4
benzaldehyde
-
in the presence of NADP+, at 25°C and pH 8.5
57
benzaldehyde
-
in the presence of NAD+, at 25°C and pH 8.5
0.13
NAD+
pH 9.0, 25°C, recombinant mutant K154A
0.45
NAD+
pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde
0.58
NAD+
pH 9.0, 25°C, recombinant mutant S157E
1.74
NAD+
pH 9.0, 25°C, recombinant wild-type enzyme
1.94
NAD+
recombinant His6-tagged enzyme, pH 7.0, 30°C
2.7
NAD+
-
in the presence of 10 mM Mg2+, at pH 7.5 and 37°C
5.26
NAD+
-
pH and temperature not specified in the publication
5.26
NAD+
pH not specified in the publication, 30°C
14
NAD+
mutant enzyme N193A, in 50 mM HEPES (pH 8.0), at 37°C
14
NAD+
mutant N193A, pH 8.0, 37°C
38
NAD+
wild-type, pH 8.0, 37°C
38
NAD+
wild type enzyme, in 50 mM HEPES (pH 8.0), at 37°C
39
NAD+
mutant enzyme K160A, in 50 mM HEPES (pH 8.0), at 37°C
39
NAD+
mutant K160A , pH 8.0, 37°C
46
NAD+
wild-type, pH 8.0, 37°C
56.8
NAD+
-
native wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C
66
NAD+
-
recombinant wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C
66
NAD+
-
His-tagged BADH
69
NAD+
-
in 0.1 M HEPES/KOH (pH 6.5), at 70°C
80
NAD+
mutant enzyme K160E, in 50 mM HEPES (pH 8.0), at 37°C
80
NAD+
mutant K160E , pH 8.0, 37°C
136.3
NAD+
-
at pH 6.5 and 70°C
176
NAD+
-
in the presence of benzaldehyde, at 25°C and pH 8.5
0.1
NADP+
pH 9.0, 25°C, recombinant mutant K154A
0.617
NADP+
pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde
1.3
NADP+
-
in the absence of Mg2+, at pH 7.5 and 37°C
1.6
NADP+
pH 9.0, 25°C, recombinant mutant S157E
2.1
NADP+
mutant enzyme K160E, in 50 mM HEPES (pH 8.0), at 37°C
2.1
NADP+
mutant K160E , pH 8.0, 37°C
2.6
NADP+
mutant enzyme K160A, in 50 mM HEPES (pH 8.0), at 37°C
2.6
NADP+
mutant K160A , pH 8.0, 37°C
3.9
NADP+
pH 9.0, 25°C, recombinant wild-type enzyme
7.2
NADP+
recombinant His6-tagged enzyme, pH 7.0, 30°C
9.93
NADP+
-
pH and temperature not specified in the publication
9.93
NADP+
pH not specified in the publication, 30°C
16.5
NADP+
-
at pH 6.5 and 70°C
17
NADP+
-
native wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C
17
NADP+
-
wild-type BADH
21
NADP+
-
His-tagged BADH
21
NADP+
mutant enzyme N193A, in 50 mM HEPES (pH 8.0), at 37°C
21
NADP+
mutant N193A, pH 8.0, 37°C
21.1
NADP+
-
recombinant wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C
40
NADP+
-
in the presence of benzaldehyde, at 25°C and pH 8.5
46
NADP+
wild type enzyme, in 50 mM HEPES (pH 8.0), at 37°C
0.1
succinate semialdehyde
pH 9.0, 25°C, recombinant mutant K154A, with NADP+
0.13
succinate semialdehyde
pH 9.0, 25°C, recombinant mutant K154A, with NAD+
0.3
succinate semialdehyde
mutant enzyme D426A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.3
succinate semialdehyde
mutant D426A , cofactor NAD+, pH 8.0, 37°C
0.483
succinate semialdehyde
pH 8.5, 30°C, recombinant enzyme, with NAD+
0.58
succinate semialdehyde
pH 9.0, 25°C, recombinant mutant S157E, with NAD+
0.583
succinate semialdehyde
pH 8.5, 30°C, recombinant enzyme, with NADP+
1.6
succinate semialdehyde
pH 9.0, 25°C, recombinant mutant S157E, with NADP+
1.74
succinate semialdehyde
pH 9.0, 25°C, recombinant wild-type enzyme, with NAD+
1.9
succinate semialdehyde
-
with NADP+ as cosubstrate, in the absence of Mg2+, at pH 7.5 and 37°C
2 - 8
succinate semialdehyde
mutant enzyme R428A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
2 - 8
succinate semialdehyde
mutant R428A , cofactor NAD+, pH 8.0, 37°C
3.9
succinate semialdehyde
pH 9.0, 25°C, recombinant wild-type enzyme, with NADP+
4.7
succinate semialdehyde
-
with NADP+ as cosubstrate, in the presence of 10 mM Mg2+, at pH 7.5 and 37°C
5.61
succinate semialdehyde
cofactor NAD+, pH not specified in the publication, 30°C
5.61
succinate semialdehyde
-
pH and temperature not specified in the publication, in presence of NAD+
7.24
succinate semialdehyde
cofactor NADP+, pH not specified in the publication, 30°C
7.24
succinate semialdehyde
-
pH and temperature not specified in the publication, in presence of NADP+
26
succinate semialdehyde
mutant enzyme F138A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
26
succinate semialdehyde
mutant F138A , cofactor NAD+, pH 8.0, 37°C
29.4
succinate semialdehyde
pH 8.0, 40°C, cosubstrate: NAD+
30
succinate semialdehyde
pH 8.0, 40°C, cosubstrate: NADP+
45
succinate semialdehyde
mutant enzyme R145A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
45
succinate semialdehyde
mutant R145A , cofactor NAD+, pH 8.0, 37°C
55
succinate semialdehyde
wild type enzyme, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
55
succinate semialdehyde
wild-type, cofactor NAD+, pH 8.0, 37°C
66
succinate semialdehyde
mutant enzyme W141A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
66
succinate semialdehyde
mutant W141A , cofactor NAD+, pH 8.0, 37°C
68
succinate semialdehyde
mutant enzyme S425A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
68
succinate semialdehyde
mutant S425A , cofactor NAD+, pH 8.0, 37°C
73
succinate semialdehyde
mutant enzyme K92A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
73
succinate semialdehyde
mutant K92A, cofactor NAD+, pH 8.0, 37°C
83
succinate semialdehyde
wild type enzyme, with NADP+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
83
succinate semialdehyde
wild-type, cofactor NADP+, pH 8.0, 37°C
164
succinate semialdehyde
mutant enzyme E442A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
164
succinate semialdehyde
mutant E442A, cofactor NAD+, pH 8.0, 37°C
16.8
Succinic semialdehyde
-
with NAD+ as cosubstrate, at pH 6.5 and 70°C
18.4
Succinic semialdehyde
-
with NADP+ as cosubstrate, at pH 6.5 and 70°C
22.6
Succinic semialdehyde
-
in 0.1 M HEPES/KOH (pH 6.5), at 70°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
134.1 - 215.3
2-oxoglutarate semialdehyde
0.36 - 14700
succinate semialdehyde
1789 - 3454
Succinic semialdehyde
134.1
2-oxoglutarate semialdehyde
-
in 0.1 M HEPES/KOH (pH 6.5), at 70°C
134.1
2-oxoglutarate semialdehyde
-
with NADP+ as cosubstrate, at pH 6.5 and 70°C
215.3
2-oxoglutarate semialdehyde
-
with NAD+ as cosubstrate, at pH 6.5 and 70°C
0.087
NAD+
pH 9.0, 25°C, recombinant mutant K154A
0.4
NAD+
pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde
1.02
NAD+
pH 9.0, 25°C, recombinant wild-type enzyme
1.14
NAD+
pH 9.0, 25°C, recombinant mutant S157E
3.8
NAD+
mutant enzyme K160A, in 50 mM HEPES (pH 8.0), at 37°C
3.8
NAD+
mutant K160A , pH 8.0, 37°C
7.3
NAD+
mutant enzyme K160E, in 50 mM HEPES (pH 8.0), at 37°C
7.3
NAD+
mutant K160E , pH 8.0, 37°C
9.7
NAD+
recombinant His6-tagged enzyme, pH 7.0, 30°C
12.3
NAD+
-
in 0.1 M HEPES/KOH (pH 6.5), at 70°C
12.3
NAD+
-
at pH 6.5 and 70°C
25.1
NAD+
-
pH and temperature not specified in the publication
25.1
NAD+
pH not specified in the publication, 30°C
95
NAD+
wild-type, pH 8.0, 37°C
97
NAD+
mutant enzyme N193A, in 50 mM HEPES (pH 8.0), at 37°C
97
NAD+
mutant N193A, pH 8.0, 37°C
290
NAD+
-
in the presence of 10 mM Mg2+, at pH 7.5 and 37°C
880
NAD+
wild-type, pH 8.0, 37°C
880
NAD+
wild type enzyme, in 50 mM HEPES (pH 8.0), at 37°C
0.016
NADP+
pH 9.0, 25°C, recombinant mutant v
0.077
NADP+
mutant enzyme K160E, in 50 mM HEPES (pH 8.0), at 37°C
0.1
NADP+
mutant enzyme K160A, in 50 mM HEPES (pH 8.0), at 37°C
0.1
NADP+
mutant K160A , pH 8.0, 37°C
0.77
NADP+
mutant K160E , pH 8.0, 37°C
1.46
NADP+
pH 9.0, 25°C, recombinant mutant S157E
8.6
NADP+
mutant enzyme N193A, in 50 mM HEPES (pH 8.0), at 37°C
8.6
NADP+
mutant N193A, pH 8.0, 37°C
25.4
NADP+
-
pH and temperature not specified in the publication
25.4
NADP+
pH not specified in the publication, 30°C
72
NADP+
recombinant His6-tagged enzyme, pH 7.0, 30°C
95
NADP+
wild type enzyme, in 50 mM HEPES (pH 8.0), at 37°C
114.7
NADP+
pH 9.0, 25°C, recombinant wild-type enzyme
154.3
NADP+
pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde
210
NADP+
-
in the absence of Mg2+, at pH 7.5 and 37°C
3066
NADP+
-
in 0.1 M HEPES/KOH (pH 6.5), at 70°C
30660
NADP+
-
at pH 6.5 and 70°C
0.36
succinate semialdehyde
cofactor NADP+, pH not specified in the publication, 30°C
0.362
succinate semialdehyde
-
pH and temperature not specified in the publication, in presence of NADP+
0.598
succinate semialdehyde
-
pH and temperature not specified in the publication, in presence of NAD+
0.6
succinate semialdehyde
cofactor NAD+, pH not specified in the publication, 30°C
1.3
succinate semialdehyde
mutant D426A , cofactor NAD+, pH 8.0, 37°C
5
succinate semialdehyde
pH 9.0, 25°C, recombinant mutant K154A, with NADP+
6.5
succinate semialdehyde
pH 9.0, 25°C, recombinant mutant K154A, with NAD+
18
succinate semialdehyde
mutant enzyme R145A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
18
succinate semialdehyde
mutant R145A , cofactor NAD+, pH 8.0, 37°C
28
succinate semialdehyde
mutant enzyme K92A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
28
succinate semialdehyde
mutant K92A, cofactor NAD+, pH 8.0, 37°C
70.4
succinate semialdehyde
pH 8.5, 30°C, recombinant enzyme, with NAD+
86
succinate semialdehyde
mutant enzyme W141A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
86
succinate semialdehyde
mutant W141A , cofactor NAD+, pH 8.0, 37°C
110
succinate semialdehyde
mutant enzyme E442A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
130
succinate semialdehyde
mutant enzyme D426A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
130
succinate semialdehyde
mutant enzyme R428A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
140
succinate semialdehyde
-
with NADP+ as cosubstrate, in the absence of Mg2+, at pH 7.5 and 37°C
180
succinate semialdehyde
wild type enzyme, with NADP+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
194.3
succinate semialdehyde
pH 8.5, 30°C, recombinant enzyme, with NADP+
200
succinate semialdehyde
wild type enzyme, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
207.1
succinate semialdehyde
pH 9.0, 25°C, recombinant mutant S157E, with NAD+
210
succinate semialdehyde
mutant enzyme F138A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
210
succinate semialdehyde
mutant F138A , cofactor NAD+, pH 8.0, 37°C
310
succinate semialdehyde
mutant enzyme S425A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
310
succinate semialdehyde
mutant S425A , cofactor NAD+, pH 8.0, 37°C
435
succinate semialdehyde
pH 9.0, 25°C, recombinant wild-type enzyme, with NAD+
487.5
succinate semialdehyde
pH 9.0, 25°C, recombinant wild-type enzyme, with NADP+
533.3
succinate semialdehyde
pH 9.0, 25°C, recombinant mutant S157E, with NADP+
1100
succinate semialdehyde
mutant E442A, cofactor NAD+, pH 8.0, 37°C
1300
succinate semialdehyde
mutant R428A , cofactor NAD+, pH 8.0, 37°C
1600
succinate semialdehyde
-
with NADP+ as cosubstrate, in the presence of 10 mM Mg2+, at pH 7.5 and 37°C
1800
succinate semialdehyde
wild-type, cofactor NADP+, pH 8.0, 37°C
2000
succinate semialdehyde
wild-type, cofactor NAD+, pH 8.0, 37°C
10300
succinate semialdehyde
pH 8.0, 60°C, cosubstrate: NADP+
14700
succinate semialdehyde
pH 8.0, 60°C, cosubstrate: NAD+
1789
Succinic semialdehyde
-
with NAD+ as cosubstrate, at pH 6.5 and 70°C
3454
Succinic semialdehyde
-
in 0.1 M HEPES/KOH (pH 6.5), at 70°C
3454
Succinic semialdehyde
-
with NADP+ as cosubstrate, at pH 6.5 and 70°C
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0.0017
-
wild type, value below, NH4+ used as N-source or uga2 mutant unable to grow on 4-aminobutyric acid, glutamate and 4-aminobutyric acid used as N-source
0.0025
-
wild type, glutamate used as N-source
0.0033
-
uga3 mutant unable to grow on 4-aminobutyric acid, glutamate and 4-aminobutyric acid used as N-source
0.0038
H16-strain, coenzyme NAD+
0.0097
SK4580-strain, coenzyme NAD+
0.0105
HF39-strain, coenzyme NAD+
0.0172
SHF3-strain, coenzyme NAD+
0.021
-
wild type, succinate used as C-source, gamma-aminobutyrate and NH3 used as N-source
0.0235
SK4580-strain, coenzyme NADP+
0.0253
H16-strain, coenzyme NADP+
0.028
-
bis(3-aminopropyl)-amine used as C-source and N-source
0.029
-
spermidine used as C-source and N-source
0.03
-
bis(3-aminopropyl)-amine and glucose, glucose and NH3 or ribose and NH3 used as C-source and N-source
0.0319
SK4575-strain, coenzyme NAD+
0.032
-
gamma-aminobutyric acid and glucose used as C-source and N-source
0.033
-
spermidine and glucose used as C-source and N-source
0.034
-
wild type, 4-hydroxyphenylacetate used as C-source and NH3 used as N-source
0.035
-
gamma-aminobutyric acid used as C-source and N-source
0.0355
SK4575-strain, coenzyme NADP+
0.036
-
CS101A strain, unable to utilize 4-aminobutyrate as N-source
0.038
-
putrescine used as C-source and N-source
0.0409
HF39-strain, coenzyme NADP+
0.045
-
gamma-hydroxybutyric acid and NH3 used as C-source and N-source
0.0457
SHF3-strain, coenzyme NADP+
0.06
-
4-hydroxyphenylacetic acid and glucose used as carbon source, NH3 used as N-source
0.07
-
succinate used as carbon source, NH3 used as N-source
0.073
-
nutrient broth used as carbon source, NADP-dependent form
0.078
-
glycerol used as carbon source, 4-aminobutyric acid used as N-source
0.08
-
4-hydroxyphenylacetic acid used as carbon source, NH3 used as N-source
0.085
-
4-aminobutyric acid used as carbon source, NH3 used as N-source
0.089
-
mutant, glucose used as C-source and NH3 used as N-source
0.091
-
4-hydroxyphenylacetic acid, glucose and cAMP used as carbon source, NH3 used as N-source
0.097
-
mutant, succinate used as C-source and NH3 used as N-source
0.105
-
wild type, succinate used as C-source and gamma-aminobutyrate used as N-source
0.125
-
uga1 mutant unable to grow on 4-aminobutyric acid, glutamate and 4-aminobutyric acid used as N-source
0.13
-
4-hydroxyphenylacetic acid and cAMP used as carbon source, NH3 used as N-source
0.319
-
mutant, gamma-aminobutyrate used as C-source and NH3 used as N-source
0.351
-
mutant, succinate used as C-source and gamma-aminobutyrate used as N-source
0.38
-
wild type, glutamate and 4-aminobutyric acid used as N-source
0.395
-
mutant, glucose used as C-source and gamma-aminobutyrate used as N-source
0.408
-
mutant, gamma-aminobutyrate used as C-source and as N-source
0.5 - 0.66
-
wild type, 4-aminobutyric acid used as N-source
0.731
-
CS101G2 strain, unable to utilize 4-aminobutyrate as N-source
0.797
-
S-5 strain, unable to utilize 4-aminobutyrate as N-source
1.012
-
S-9 strain, unable to utilize 4-aminobutyrate as N-source
1.023
-
L-18 strain, unable to utilize 4-aminobutyrate as N-source
1.038
-
D-8 strain, unable to utilize 4-aminobutyrate as N-source
1.08
-
M-20 strain, unable to utilize 4-aminobutyrate as N-source
1.264
-
CS101B strain, able to utilize 4-aminobutyrate as N-source
0.023
-
wild type, succinate used as C-source and proline used as N-source
0.023
-
putrescine and glucose used as C-source and N-source
0.026
-
wild type, succinate used as C-source and NH3 used as N-source
0.026
-
casamino acids used as C-source and N-source
0.075
-
glycerol used as carbon source, NH3 used as N-source
0.075
-
wild type, NH4+ and 4-aminobutyric acid used as N-source
8.5
-
-
additional information
-
-
additional information
-
-
additional information
specific activity of 0.3 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is sulfopropanal and NADP+
additional information
-
specific activity of 0.3 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is sulfopropanal and NADP+
additional information
specific activity of 0.5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is succinale semialdehyde and NAD+
additional information
-
specific activity of 0.5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is succinale semialdehyde and NAD+
additional information
specific activity of 0.5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is succinale semialdehyde and NADP+
additional information
-
specific activity of 0.5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is succinale semialdehyde and NADP+
additional information
specific activity of 0.6 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is sulfopropanal and NAD+
additional information
-
specific activity of 0.6 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is sulfopropanal and NAD+
additional information
specific activity of 0.7 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is succinale semialdehyde and NADP+
additional information
-
specific activity of 0.7 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is succinale semialdehyde and NADP+
additional information
specific activity of 10 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is sulfopropanal and NADP+
additional information
-
specific activity of 10 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is sulfopropanal and NADP+
additional information
specific activity of 2.5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is sulfopropanal and NADP+
additional information
-
specific activity of 2.5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is sulfopropanal and NADP+
additional information
specific activity of 3 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is sulfopropanal and NAD+
additional information
-
specific activity of 3 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is sulfopropanal and NAD+
additional information
specific activity of 5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is sulfopropanal and NAD+
additional information
-
specific activity of 5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is sulfopropanal and NAD+
additional information
specific activity of 5.0 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is succinale semialdehyde and NAD+
additional information
-
specific activity of 5.0 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is succinale semialdehyde and NAD+
additional information
specific activity of 7.0 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is succinale semialdehyde and NADP+
additional information
-
specific activity of 7.0 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is succinale semialdehyde and NADP+
additional information
specific activity of 7.3 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is succinale semialdehyde and NAD+
additional information
-
specific activity of 7.3 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is succinale semialdehyde and NAD+
additional information
-
-
additional information
-
Good activity with several alternate substrates including the aromatic substrates, 4-chloro- and 3-hydroxy-benzaldehyde, as well as cyclohexanal. BADH is most active with medium chain aliphatic substrates such as pentanal and hexanal.The level of activity with aliphatic substrates drops off rapidly as the chain length decreased with very little activity (<0.1%) being observed with acetaldehyde.
additional information
-
-
additional information
-
-
additional information
-
-
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metabolism
GABA metabolism
metabolism
-
succinic semialdehyde dehydrogenase (SSADH) catalyzes the oxidation of succinic semialdehyde (SSA) into succinic acid in the final step of gamma-aminobutyric acid degradation
metabolism
succinic semialdehyde dehydrogenase (SSADH) catalyzes the oxidation of succinic semialdehyde to succinic acid in the final step of GABA catabolism
metabolism
the enhanced production of 2-oxoglutarate (KG) effected by Pseudomonas fluorescens in a mineral medium supplemented with manganese (Mn) is propelled by the increased activities of succinate semialdehyde dehydrogenase (SSADH), gamma-aminobutyric acid aminotransaminase (GABAT), and isocitrate lyase (ICL). The latter generates glyoxylate and succinate two key metabolites involved in this process. Fumarate reductase (FRD) also aids in augmenting the pool of succinate, a precursor of succinate semialdehyde (SSA). The latter is then carboxylated to KG with the assistance of 2-oxoglutarate decarboxylase (KDC)
metabolism
-
succinic semialdehyde dehydrogenase (SSADH) catalyzes the oxidation of succinic semialdehyde (SSA) into succinic acid in the final step of gamma-aminobutyric acid degradation
-
metabolism
-
the enhanced production of 2-oxoglutarate (KG) effected by Pseudomonas fluorescens in a mineral medium supplemented with manganese (Mn) is propelled by the increased activities of succinate semialdehyde dehydrogenase (SSADH), gamma-aminobutyric acid aminotransaminase (GABAT), and isocitrate lyase (ICL). The latter generates glyoxylate and succinate two key metabolites involved in this process. Fumarate reductase (FRD) also aids in augmenting the pool of succinate, a precursor of succinate semialdehyde (SSA). The latter is then carboxylated to KG with the assistance of 2-oxoglutarate decarboxylase (KDC)
-
physiological function
enzyme GabD irreversibly oxidizes D-glyceraldehyde 3-phosphate (Ga3P) to 3-phospho-D-glycerate (3Pglycerate) using NAD+ or NADP+, thus resembling a non-phosphorylating Ga3PDHase (EC 1.2.1.90). But the enzyme shows about 6fold higher Km value and three orders of magnitude higher catalytic efficiency with succinate semialdehyde (SSA) and NADP+. Indeed, the GabD protein identity corresponds to an SSA dehydrogenase (SSADHase). As an SSADHase, GabD physiologically acts producing succinate and preferentially NADPH over NADH, thus being part of an alternative pathway of the tricarboxylic acid cycle converting alpha-ketoglutarate to succinate
physiological function
-
enzyme GabD irreversibly oxidizes D-glyceraldehyde 3-phosphate (Ga3P) to 3-phospho-D-glycerate (3Pglycerate) using NAD+ or NADP+, thus resembling a non-phosphorylating Ga3PDHase (EC 1.2.1.90). But the enzyme shows about 6fold higher Km value and three orders of magnitude higher catalytic efficiency with succinate semialdehyde (SSA) and NADP+. Indeed, the GabD protein identity corresponds to an SSA dehydrogenase (SSADHase). As an SSADHase, GabD physiologically acts producing succinate and preferentially NADPH over NADH, thus being part of an alternative pathway of the tricarboxylic acid cycle converting alpha-ketoglutarate to succinate
-
physiological function
-
enzyme GabD irreversibly oxidizes D-glyceraldehyde 3-phosphate (Ga3P) to 3-phospho-D-glycerate (3Pglycerate) using NAD+ or NADP+, thus resembling a non-phosphorylating Ga3PDHase (EC 1.2.1.90). But the enzyme shows about 6fold higher Km value and three orders of magnitude higher catalytic efficiency with succinate semialdehyde (SSA) and NADP+. Indeed, the GabD protein identity corresponds to an SSA dehydrogenase (SSADHase). As an SSADHase, GabD physiologically acts producing succinate and preferentially NADPH over NADH, thus being part of an alternative pathway of the tricarboxylic acid cycle converting alpha-ketoglutarate to succinate
-
physiological function
-
enzyme GabD irreversibly oxidizes D-glyceraldehyde 3-phosphate (Ga3P) to 3-phospho-D-glycerate (3Pglycerate) using NAD+ or NADP+, thus resembling a non-phosphorylating Ga3PDHase (EC 1.2.1.90). But the enzyme shows about 6fold higher Km value and three orders of magnitude higher catalytic efficiency with succinate semialdehyde (SSA) and NADP+. Indeed, the GabD protein identity corresponds to an SSA dehydrogenase (SSADHase). As an SSADHase, GabD physiologically acts producing succinate and preferentially NADPH over NADH, thus being part of an alternative pathway of the tricarboxylic acid cycle converting alpha-ketoglutarate to succinate
-
physiological function
-
enzyme GabD irreversibly oxidizes D-glyceraldehyde 3-phosphate (Ga3P) to 3-phospho-D-glycerate (3Pglycerate) using NAD+ or NADP+, thus resembling a non-phosphorylating Ga3PDHase (EC 1.2.1.90). But the enzyme shows about 6fold higher Km value and three orders of magnitude higher catalytic efficiency with succinate semialdehyde (SSA) and NADP+. Indeed, the GabD protein identity corresponds to an SSA dehydrogenase (SSADHase). As an SSADHase, GabD physiologically acts producing succinate and preferentially NADPH over NADH, thus being part of an alternative pathway of the tricarboxylic acid cycle converting alpha-ketoglutarate to succinate
-
additional information
the conserved Cys262 and Glu228 residues are crucial for the catalytic activity of cce4228 protein and the Ser157 and Lys154 residues are determinants of cofactor preference. The Cys residue is thought to function as a nucleophile in the catalytic mechanism. Homology structure modeling of wild-type cce4228 protein
additional information
-
the conserved Cys262 and Glu228 residues are crucial for the catalytic activity of cce4228 protein and the Ser157 and Lys154 residues are determinants of cofactor preference. The Cys residue is thought to function as a nucleophile in the catalytic mechanism. Homology structure modeling of wild-type cce4228 protein
-
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Nirenberg, M.W.; Jakoby, W.B.
Enzymatic utilization of gamma-hydroxybutyric acid
J. Biol. Chem.
235
954-960
1960
Pseudomonas sp.
brenda
Ramos, F.; El Guezzar, M.; Grenson, M.; Wiame, J.M.
Mutations affecting the enzymes involved in the utilization of 4-aminobutyric acid as nitrogen source by the yeast Saccharomyces cerevisiae
Eur. J. Biochem.
149
401-404
1985
Saccharomyces cerevisiae
brenda
Sanchez, M.; Fernandez, J.; Martin, M.; Gibello, A.; Garrido-Pertierra, A.
Purification and properties of two succinic semialdehyde dehydrogenases from Klebsiella pneumoniae
Biochim. Biophys. Acta
990
225-231
1989
Klebsiella pneumoniae
brenda
Donelly, M.I.; Cooper, R.A.
Succinic semialdehyde dehydrogenases of Escherichia coli: their role in the degradation of p-hydroxyphenylacetate and gamma-aminobutyrate
Eur. J. Biochem.
113
555-561
1981
Escherichia coli
brenda
Blakley, E.R.
The catabolism of L-tyrosine by an Arthrobacter sp.
Can. J. Microbiol.
23
1128-1139
1977
Arthrobacter sp.
brenda
Jakoby, W.B.
Enzymes of gamma-aminobutyrate metabolism (bacterial)
Methods Enzymol.
5
765-778
1962
Pseudomonas fluorescens
-
brenda
Tokunaga, M.; Nakano, Y.; Kitaoka, S.
Separation and properties of the NAD-linked and NADP-linked isozymes of succinic semialdehyde dehydrogenase in Euglena gracilis z
Biochim. Biophys. Acta
429
55-62
1976
Euglena gracilis
brenda
Dover, S.; Halpern, Y.S.
Novel type of catabolite repression in the pathway of gamma-aminobutyrate breakdown in Escherichia coli K-12
FEBS Lett.
37
207-211
1973
Escherichia coli
brenda
Yambe, R.; Hukui, T.; Tuboi, S.
Succinate semialdehyde dehydrogenase of Rhodopseudomonas spheroides which is active with both NADP+ and NAD+
J. Biochem.
70
243-247
1971
Cereibacter sphaeroides
brenda
Padmanabhan, R.; Tchen, T.T.
Nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate-linked succinic semialdehyde dehydrogenases in a Pseudonomas species
J. Bacteriol.
100
398-402
1969
Pseudomonas sp.
brenda
Jakoby, W.B.; Scott, E.M.
Aldehyde oxidation III. Succinic semialdehyde dehydrogenase
J. Biol. Chem.
234
937-940
1959
Pseudomonas fluorescens
brenda
Sims, K.L.; Davis, G.A.
Subcellular distribution of succinate-semialdehyde dehydrogenase in rat brain
Eur. J. Biochem.
35
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