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2,5-dioxopentanoate + NAD+ + H2O
?
2,5-dioxopentanoate + NADP+ + H2O
?
3-carboxybenzaldehyde + NADP+ + H2O
3-carboxybenzoate + NADPH + 2 H+
-
-
-
?
3-nitrobenzaldehyde + NADP+ + H2O
3-nitrobenzoate + NADPH + 2 H+
-
-
-
?
4-carboxybenzaldehyde + NADP+ + H2O
4-carboxybenzoate + NADPH + H+
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + 2 H+
-
-
-
?
glutaric semialdehyde + NADP+ + H2O
glutarate + NADPH + 2 H+
-
-
-
?
malonate semialdehyde + NADP+ + H2O
malonate + NADPH + 2 H+
-
8.7% of the activity with succinate semialdehyde
-
-
?
n-butanal + NADP+ + H2O
butanoate + NADPH + 2 H+
-
-
-
?
n-hexanal + NADP+ + H2O
hexanoate + NADPH + H+
-
-
-
?
n-pentanal + NADP+ + H2O
n-pentanoate + NADPH + 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 + NADP+ + H2O
succinate + NADPH + 2 H+
additional information
?
-
2,5-dioxopentanoate + NAD+ + H2O
?
-
-
-
?
2,5-dioxopentanoate + NAD+ + H2O
?
-
-
-
?
2,5-dioxopentanoate + NADP+ + H2O
?
-
-
-
?
2,5-dioxopentanoate + NADP+ + H2O
?
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
about 11% of the activity with NADP+
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
very low activity with wild-type enzyme, higher activity with enzyme mutants S157E and S157P
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
poor cofactor for the wild-type enzyme, but is utilized by enzyme mutants, overview
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
kcat/Km for NADP+ is 250fold higher compared to kcat/Km for NAD+
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
kcat/Km for NADP+ is 250fold higher compared to kcat/Km for NAD+
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
-
-
?
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+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
preferred substrates
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
specific for
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
kcat/Km for NADP+ is 250fold higher compared to kcat/Km for NAD+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
kcat/Km for NADP+ is 250fold higher compared to kcat/Km for NAD+
-
-
?
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+
data from crystal structures provide details about the catalytic mechanism by revealing a covalent adduct of a cofactor with the catalytic cysteine in the binary complex and a proposed thiohemiacetal intermediate in the ternary complex
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
binding structure, overview
-
-
r
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
r
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
binding structure, overview
-
-
r
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
-
-
?
succinic semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
chemical mechanism based on functional data and structural information proposed, 1H-NMR to probe the stereospecificity of GabD1 show a transfer of the deuteride to the pro-R position of NADP+ indicating GabD1 has A-type stereospecificity
-
-
ir
succinic semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
chemical mechanism based on functional data and structural information proposed, 1H-NMR to probe the stereospecificity of GabD1 show a transfer of the deuteride to the pro-R position of NADP+ indicating GabD1 has A-type stereospecificity
-
-
ir
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
-
-
?
additional information
?
-
-
no substrate: n-butanal, formaldehyde, acetaldehyde, glyoxal, glyoxalate, propanal, glutaraldehyde, benzaldehyde, and anisaldehyde
-
-
?
additional information
?
-
-
no substrate: glyoxylic acid, formic acid, formaldehyde, acetaldehyde, glyoxal, furfural and acrolein
-
-
?
additional information
?
-
other aldehydes, such as formaldehyde, acetaldehyde and glutaraldehyde, are very poor substrates showing a narrow substrate specificity of GabD1
-
-
?
additional information
?
-
other aldehydes, such as formaldehyde, acetaldehyde and glutaraldehyde, are very poor substrates showing a narrow substrate specificity of GabD1
-
-
?
additional information
?
-
glutaric semialdehyde (GRSAL) is the second-best substrate, but it is oxidized at only 1.2% rate compared with succinate semialdehyde
-
-
-
additional information
?
-
-
glutaric semialdehyde (GRSAL) is the second-best substrate, but it is oxidized at only 1.2% rate compared with succinate semialdehyde
-
-
-
additional information
?
-
in the binary enzyme-succinate semialdehyde-complex of SpSSADH, the succinate semialdehyde shows a tightly bound bent form nearby the catalytic residues, which may be caused by reduction of the cavity volume for substrate binding, compared with other SSADHs. Structural comparison of the tertiary enzyme-succinate semialdehyde-NADP+-complex with a binary complex + of SpSSADH with NADP indicates that the substrate inhibition is induced by the binding of inhibitory succinate semialdehyde in the cofactor-binding site, instead of NADP+. In the active site of enzyme SpSSADH, SSA is buried inside of the substrate-binding pocket formed by Phe133, Tyr136, Val262, Trp418 and Phe426 residues, substrate binding structure, overview
-
-
?
additional information
?
-
in the binary enzyme-succinate semialdehyde-complex of SpSSADH, the succinate semialdehyde shows a tightly bound bent form nearby the catalytic residues, which may be caused by reduction of the cavity volume for substrate binding, compared with other SSADHs. Structural comparison of the tertiary enzyme-succinate semialdehyde-NADP+-complex with a binary complex + of SpSSADH with NADP indicates that the substrate inhibition is induced by the binding of inhibitory succinate semialdehyde in the cofactor-binding site, instead of NADP+. In the active site of enzyme SpSSADH, SSA is buried inside of the substrate-binding pocket formed by Phe133, Tyr136, Val262, Trp418 and Phe426 residues, substrate binding structure, overview
-
-
?
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succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
succinic semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
-
-
?
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+
data from crystal structures provide details about the catalytic mechanism by revealing a covalent adduct of a cofactor with the catalytic cysteine in the binary complex and a proposed thiohemiacetal intermediate in the ternary complex
-
-
?
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 + H+
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
-
-
?
succinic semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
chemical mechanism based on functional data and structural information proposed, 1H-NMR to probe the stereospecificity of GabD1 show a transfer of the deuteride to the pro-R position of NADP+ indicating GabD1 has A-type stereospecificity
-
-
ir
succinic semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
chemical mechanism based on functional data and structural information proposed, 1H-NMR to probe the stereospecificity of GabD1 show a transfer of the deuteride to the pro-R position of NADP+ indicating GabD1 has A-type stereospecificity
-
-
ir
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NADPH
binding structure, overview
NAD+
about 11% of the activity with NADP+
NAD+
NAD+ acts as cosubstrate, but the reaction rates are more than 20fold lower than those with NADP+
NAD+
NADP+ is preferred over NAD+
NAD+
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
NAD+
kcat/Km for NADP+ is 250fold higher compared to kcat/Km for NAD+
NAD+
long incubations lead to modest utilization
NAD+
preferred cofactor for enzyme mutants S157E and S157P compared to wild-type enzyme
NADP+
-
-
NADP+
preferred substrate
NADP+
-
specific for NADP+
NADP+
-
specific for NADP+
NADP+
cofactor binding structure, overview
NADP+
electron density analysis of binding site. The enzyme activity measured in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
NADP+
-
enzyme is specific for NADP+ as a cofactor
NADP+
NAD+ also acts as cosubstrate, but the reaction rates are more than 20fold lower than those with NADP+
NADP+
NADP+ is preferred over NAD+
NADP+
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
NADP+
kcat/Km for NADP+ is 250fold higher compared to kcat/Km for NAD+
NADP+
enzyme activity increases significantly, and the enzyme becomes resistant to oxidative stress in presence of NADP+ and DTT
NADP+
Ser157 residue in Sp2771 plays a critical structural role in determining NADP+ preference for Sp2771, whereas size and distribution of hydrophobic residues along the substrate binding funnel determine substrate selection
NADP+
preferred cofactor, structural comparison between the apoform and the coenzyme complex reveal that NADP+ binding induces a conformational change of the loop carrying Arg228, which seals the NADP+ in the coenzyme cavity via its 2'-phosphate and alpha-phosphate groups. The presence of a serine residue (Ser197) in PpALDH21 allows for binding of the 2'-phosphate group of NADP+
NADP+
preferred cofactor, the Glu228 residue is located in the NADP+ binding pocket
additional information
no cofactor: NAD+
-
additional information
no detectable activity by using NAD+ as cofactor
-
additional information
AbSSADH can use both NADP+ and NAD+ as electron acceptors but has a greater preference for NADP+. The specific activity of the enzyme with NADP+ is 10times higher than that with NAD+. Residue Ser183 is involved in cofactor binding
-
additional information
-
AbSSADH can use both NADP+ and NAD+ as electron acceptors but has a greater preference for NADP+. The specific activity of the enzyme with NADP+ is 10times higher than that with NAD+. Residue Ser183 is involved in cofactor binding
-
additional information
ApSSADH prefers to use NADP+ rather than NAD+ as its cofactor. Residue Ser157 of ApSSADH plays a critical role in determining the cofactor preference. The catalytic activities of mutants S157E and S157P are elevated when the cofactor is switched from NADP+ to NAD+
-
additional information
NAD+ is a very poor coenzyme for ALDH21, the activity with NAD+ is only about 3% of that with NADP+
-
additional information
-
NAD+ is a very poor coenzyme for ALDH21, the activity with NAD+ is only about 3% of that with NADP+
-
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0.1 - 0.2
2,5-dioxopentanoate
0.551
Glutaric semialdehyde
recombinant wild-type enzyme, pH 8.2, 25°C, with NADP+
0.001 - 3.95
succinate semialdehyde
0.003 - 0.0133
Succinic semialdehyde
additional information
additional information
-
0.1
2,5-dioxopentanoate
pH 6.5, 70°C, cofactor NAD+
0.2
2,5-dioxopentanoate
pH 6.5, 70°C, cofactor NADP+
0.23
NAD+
pH 7.0, 30°C
4.49
NAD+
pH 9.5, 25°C, recombinant mutant S157E
5.37
NAD+
recombinant wild-type enzyme, pH 8.2, 25°C, with succinate semialdehyde
5.98
NAD+
pH 9.5, 25°C, recombinant mutant S157P
8.44
NAD+
recombinant mutant R228A, pH 8.2, 25°C, with succinate semialdehyde
16.1
NAD+
pH 9.5, 25°C, recombinant wild-type enzyme
0.0092
NADP+
steady-state parameter, 50 microM NADP+ and 10 mM Mg2+, at pH 7.5 and 37°C
0.024
NADP+
recombinant wild-type enzyme, pH 8.2, 25°C, with succinate semialdehyde
0.038
NADP+
-
pH 8.7, 35°C
0.04
NADP+
-
pH 9.0, 37°C
0.0446
NADP+
pH 8.5, 22°C
0.058
NADP+
pH 9.7, 45°C, recombinant detagged enzyme
0.0613
NADP+
steady-state parameter, 50 microM NADP+, at pH 7.5 and 37°C
0.1
NADP+
pH 9.5, 25°C, recombinant wild-type enzyme
0.135
NADP+
-
pH 8.0, 30°C
0.25
NADP+
-
pH 7.8, 30°C
0.375
NADP+
recombinant mutant R228A, pH 8.2, 25°C, with succinate semialdehyde
10.4
NADP+
pH 9.5, 25°C, recombinant mutant S157E
12.9
NADP+
pH 9.5, 25°C, recombinant mutant S157P
0.001
succinate semialdehyde
pH 6.5, 70°C, cofactor NAD+
0.00395
succinate semialdehyde
recombinant enzyme, pH 7.0, 30°C
0.004
succinate semialdehyde
pH 6.5, 70°C, cofactor NADP+
0.0078
succinate semialdehyde
pH 8.5, 22°C
0.01
succinate semialdehyde
-
pH 9.0, 37°C
0.01
succinate semialdehyde
pH 9.7, 45°C, recombinant detagged enzyme
0.01694
succinate semialdehyde
pH 8.0, 30°C
0.01694
succinate semialdehyde
in 100 mM sodium phosphate buffer, pH 8.0, 30°C
0.0199
succinate semialdehyde
-
pH 8.0, 30°C
0.04
succinate semialdehyde
-
pH 7.8, 30°C
0.127
succinate semialdehyde
recombinant mutant R228A, pH 8.2, 25°C, with NADP+
0.127
succinate semialdehyde
recombinant mutant Y296A, pH 8.2, 25°C, with NADP+
0.135
succinate semialdehyde
recombinant mutant R457A, pH 8.2, 25°C, with NADP+
0.181
succinate semialdehyde
recombinant wild-type enzyme, pH 8.2, 25°C, with NADP+
0.189
succinate semialdehyde
pH 8.0, 25°C
0.268
succinate semialdehyde
recombinant mutant R121A, pH 8.2, 25°C, with NADP+
1.06
succinate semialdehyde
-
pH 8.7, 35°C
1.49
succinate semialdehyde
recombinant mutant N175A, pH 8.2, 25°C, with NADP+
3.95
succinate semialdehyde
pH 7.0, 30°C
0.003
Succinic semialdehyde
steady-state parameter, 200 microM succinic semialdehyde and 10 mM Mg2+, at pH 7.5 and 37°C
0.0133
Succinic semialdehyde
steady-state parameter, 200 microM succinic semialdehyde, at pH 7.5 and 37°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
enzyme does not obey Michaelis-Menten kinetics
-
additional information
additional information
the Km-value of succinate semialdehyde estimated to be far less than 0.05 mM
-
additional information
additional information
steady-state kinetic analysis. Pre-steady-state kinetics show burst kinetics for NADPH formation in SSADH, indicating that the rate-limiting step is associated with steps that occur after the hydride transfer. Detection of burst kinetics of NADPH production by pre-steady-state analysis indicates that the rate-limiting step of the AbSSADH reaction occurs after the hydride transfer step
-
additional information
additional information
-
steady-state kinetic analysis. Pre-steady-state kinetics show burst kinetics for NADPH formation in SSADH, indicating that the rate-limiting step is associated with steps that occur after the hydride transfer. Detection of burst kinetics of NADPH production by pre-steady-state analysis indicates that the rate-limiting step of the AbSSADH reaction occurs after the hydride transfer step
-
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21.2 - 27.3
2,5-dioxopentanoate
0.27
Glutaric semialdehyde
recombinant wild-type enzyme, pH 8.2, 25°C, with NADP+
0.02 - 137
succinate semialdehyde
1.9 - 4.7
Succinic semialdehyde
21.2
2,5-dioxopentanoate
pH 6.5, 70°C, cofactor NADP+
27.3
2,5-dioxopentanoate
pH 6.5, 70°C, cofactor NAD+
1.2
NAD+
recombinant mutant R228A, pH 8.2, 25°C, with succinate semialdehyde
3.3
NAD+
recombinant wild-type enzyme, pH 8.2, 25°C, with succinate semialdehyde
1.3
NADP+
steady-state parameter, 50 microM NADP+, at pH 7.5 and 37°C
2.7
NADP+
steady-state parameter, 50 microM NADP+ and 10 mM Mg2+, at pH 7.5 and 37°C
6.4
NADP+
recombinant mutant R228A, pH 8.2, 25°C, with succinate semialdehyde
15.2
NADP+
recombinant wild-type enzyme, pH 8.2, 25°C, with succinate semialdehyde
0.02
succinate semialdehyde
recombinant mutant R121A, pH 8.2, 25°C, with NADP+
0.02
succinate semialdehyde
recombinant mutant R457A, pH 8.2, 25°C, with NADP+
1.38
succinate semialdehyde
pH 9.7, 45°C, recombinant detagged enzyme
1.69
succinate semialdehyde
recombinant enzyme, pH 7.0, 30°C
1.69
succinate semialdehyde
pH 7.0, 30°C
5.7
succinate semialdehyde
recombinant mutant R228A, pH 8.2, 25°C, with NADP+
7.1
succinate semialdehyde
recombinant mutant Y296A, pH 8.2, 25°C, with NADP+
12.5
succinate semialdehyde
recombinant mutant N175A, pH 8.2, 25°C, with NADP+
15.8
succinate semialdehyde
recombinant wild-type enzyme, pH 8.2, 25°C, with NADP+
16.8
succinate semialdehyde
pH 6.5, 70°C, cofactor NAD+
18.4
succinate semialdehyde
pH 6.5, 70°C, cofactor NADP+
137
succinate semialdehyde
pH 8.0, 25°C
1.9
Succinic semialdehyde
steady-state parameter, 200 microM succinic semialdehyde, at pH 7.5 and 37°C
4.7
Succinic semialdehyde
steady-state parameter, 200 microM succinic semialdehyde and 10 mM Mg2+, at pH 7.5 and 37°C
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134.1 - 215.3
2,5-dioxopentanoate
0.49
Glutaric semialdehyde
recombinant wild-type enzyme, pH 8.2, 25°C, with NADP+
0.075 - 3454
succinate semialdehyde
140 - 1600
Succinic semialdehyde
134.1
2,5-dioxopentanoate
pH 6.5, 70°C, cofactor NADP+
215.3
2,5-dioxopentanoate
pH 6.5, 70°C, cofactor NAD+
0.142
NAD+
recombinant mutant R228A, pH 8.2, 25°C, with succinate semialdehyde
0.615
NAD+
recombinant wild-type enzyme, pH 8.2, 25°C, with succinate semialdehyde
192
NAD+
pH 9.5, 25°C, recombinant mutant S157E
300
NAD+
pH 9.5, 25°C, recombinant mutant S157P
7.2
NADP+
pH 7.0, 30°C
17.07
NADP+
recombinant mutant R228A, pH 8.2, 25°C, with succinate semialdehyde
21
NADP+
steady-state parameter, 50 microM NADP+, at pH 7.5 and 37°C
23.8
NADP+
pH 9.7, 45°C, recombinant detagged enzyme
52.8
NADP+
pH 9.5, 25°C, recombinant mutant S157E
126
NADP+
pH 9.5, 25°C, recombinant mutant S157P
290
NADP+
steady-state parameter, 50 microM NADP+ and 10 mM Mg2+, at pH 7.5 and 37°C
633.3
NADP+
recombinant wild-type enzyme, pH 8.2, 25°C, with succinate semialdehyde
1212.4
NADP+
pH 8.0, 25°C
0.075
succinate semialdehyde
recombinant mutant R121A, pH 8.2, 25°C, with NADP+
0.148
succinate semialdehyde
recombinant mutant R457A, pH 8.2, 25°C, with NADP+
0.43
succinate semialdehyde
pH 7.0, 30°C
8.39
succinate semialdehyde
recombinant mutant N175A, pH 8.2, 25°C, with NADP+
44.88
succinate semialdehyde
recombinant mutant R228A, pH 8.2, 25°C, with NADP+
55.91
succinate semialdehyde
recombinant mutant Y296A, pH 8.2, 25°C, with NADP+
87.29
succinate semialdehyde
recombinant wild-type enzyme, pH 8.2, 25°C, with NADP+
138
succinate semialdehyde
pH 9.7, 45°C, recombinant detagged enzyme
426
succinate semialdehyde
recombinant enzyme, pH 7.0, 30°C
724.9
succinate semialdehyde
pH 8.0, 25°C
1789
succinate semialdehyde
pH 6.5, 70°C, cofactor NAD+
3454
succinate semialdehyde
pH 6.5, 70°C, cofactor NADP+
140
Succinic semialdehyde
steady-state parameter, 200 microM succinic semialdehyde, at pH 7.5 and 37°C
1600
Succinic semialdehyde
steady-state parameter, 200 microM succinic semialdehyde and 10 mM Mg2+, at pH 7.5 and 37°C
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malfunction
both R121A and R457A variants are almost inactive, demonstrating a key role of each arginine in catalysis
evolution
SSADH belongs to the aldehyde dehydrogenase (ALDH) superfamily
evolution
sequence analysis of AbSSADH reveals its high degree of sequence similarity to other enzymes in the two-cysteine GabD family
evolution
SSADH belongs to the aldehyde dehydrogenase (ALDH) superfamily, which is a kind of NAD(P)+-dependent oxidoreductase using a wide range of aldehydes as its substrate
evolution
-
SSADH belongs to the aldehyde dehydrogenase (ALDH) superfamily
-
metabolism
SSADH plays an essential role in the metabolism of the inhibitory neurotransmitter c-aminobutyric acid
metabolism
enzyme catalyzes the last step of the gamma-aminobutyrate degradation
metabolism
Sp2771 enzyme completes together with a novel 2-oxoglutarate decarboxylase a non-canonical tricarboxylic acid cycle
metabolism
succinic semialdehyde dehydrogenase from Synechococcus is an essential enzyme in the tricarboxylic acid cycle of cyanobacteria
metabolism
SySSADH catalyzes one of the NAD(P)H generating reactions in the oxidative TCA cycle. The oxidative TCA cycle is a pathway with low efficiency in NADPH generation in Synechocystis sp. 6803. Similar to isocitrate dehydrogenase from Synechocystis sp. 6803, SySSADH specifically catalyzes the NADPH-generating reaction and is not inhibited by citrate. To avoid NADPH overproduction, the oxidative pentose phosphate (OPP) pathway dehydrogenase activity is repressed when the flow of the oxidative TCA cycle increases in Synechocystis sp. 6803. Metabolic map around the OPP pathway, overview
metabolism
the enzyme is involved in the GABA shunt pathway, GABA shunt reactions from glutamate to succinate might appear in cytosol in addition to mitochondria making the GABA shunt pathway much more diverse
metabolism
the ssadh gene from Acinetobacter baumannii is part of the 4-hydroxyphenylacetate (4-HPA) degradation pathway in which SSADH converts SSA to succinic acid before entering the main metabolic TCA cycle
metabolism
-
enzyme catalyzes the last step of the gamma-aminobutyrate degradation
-
metabolism
-
SSADH plays an essential role in the metabolism of the inhibitory neurotransmitter c-aminobutyric acid
-
physiological function
gene is disrupted in a transposon-induced mutant of Ralstonia eutropha exhibiting the phenotype 4-hydroxybutyric acid-leaky
physiological function
succinic semialdehyde dehydrogenase from Synechococcus is an essential enzyme in the tricarboxylic acid, TCA, cycle of cyanobacteria. It completes a 2-oxoglutarate dehydrogenase-deficient cyanobacterial TCA cycle through a detour metabolic pathway. SySSADH produces succinate in an NADP+ -dependent manner with a single cysteine acting as the catalytic residue in the catalytic loop
physiological function
ALDH21 from the moss Physcomitrella patens codes for a tetrameric NADP+-dependent succinic semialdehyde dehydrogenase (SSALDH), which converts succinate semialdehyde, an intermediate of the gamma-aminobutyric acid (GABA) shunt pathway, into succinate in the cytosol
physiological function
production of glutaric acid depends on the expression of native gabT (EC 2.6.1.48) and gabD of Corynebacterium glutamicum, or on heterologous expression of davT (EC 2.6.1.48) and davD (EC 1.2.1.20) from Pseudomonas putida encoding 5-aminovalerate aminotransferase, and glutarate semialdehyde, respectively
physiological function
succinic semialdehyde dehydrogenase (SSADH) from Synechocystis 6803 (SySSADH) catalyzes one of the NAD(P)H generating reactions in the oxidative TCA cycle. Similar to isocitrate dehydrogenase from Synechocystis sp. 6803, SySSADH specifically catalyzes the NADPH-generating reaction and is not inhibited by citrate. The activity of SySSADH is lower than that of other bacterial SSADHs
physiological function
-
succinic semialdehyde dehydrogenase from Synechococcus is an essential enzyme in the tricarboxylic acid, TCA, cycle of cyanobacteria. It completes a 2-oxoglutarate dehydrogenase-deficient cyanobacterial TCA cycle through a detour metabolic pathway. SySSADH produces succinate in an NADP+ -dependent manner with a single cysteine acting as the catalytic residue in the catalytic loop
-
additional information
Ser157 residue in Sp2771 plays a critical structural role in determining NADP+ preference for Sp2771, whereas size and distribution of hydrophobic residues along the substrate binding funnel determine substrate selection. Enzyme Sp2771 structure modelling comprising residues 2-454, active site and substrate binding structures, overview
additional information
structure analysis of the enzyme in binary and ternary with NADP(H) and/or substrate reveals that the enzyme forms a distinct reaction intermediate in each complex: a covalent adduct of a cofactor with the catalytic cysteine in the binary complex and a proposed thiohemiacetal intermediate in the ternary complex. SySSADH produces succinate in an NADP+ -dependent manner with a single cysteine acting as the catalytic residue in the catalytic loop, catalytic mechanism, overview. The formation of the NADP-cysteine adduct is a kinetically preferred event that protects the catalytic cysteine from H2O2-dependent oxidative stress. SySSADH shows a cofactor-dependent oxidation protection in 1-Cys SSADH, which is unique relative to other 2-Cys SSADHs employing a redox-dependent formation of a disulfide bridge. The catalytic cysteine preferentially forms an NADP-cysteine adduct if NADP+ is present
additional information
AbSSADH contains a total of five cysteine residues in one subunit (Cys175, Cys245, Cys289, Cys291 and Cys479), the enzyme has two conserved cysteines, Cys289 and Cys291. Cys289 is the active residue participating in catalysis. Method devlopment to specifically measure the active site cysteine pKa without interference from other cysteines, overview. As the magnitude of burst kinetics represents the amount of NADPH formed during the first turnover, it is directly dependent on the amount of the deprotonated form of cysteine. The pKa of Cys289 was calculated from a plot of the burst magnitude vs. pH as 7.4. The Cys289 pKa is also measured based on the ability of AbSSADH to form an NADP-cysteine adduct, which can be detected by the increase of absorbance at about 330 nm as 7.9. The lowering of the catalytic cysteine pKa by 0.6-1.0 unit renders the catalytic thiol more nucleophilic, which facilitates AbSSADH catalysis under physiological conditions. Deprotonation of the ligand or an active site residue is required for the SSADH reaction
additional information
-
AbSSADH contains a total of five cysteine residues in one subunit (Cys175, Cys245, Cys289, Cys291 and Cys479), the enzyme has two conserved cysteines, Cys289 and Cys291. Cys289 is the active residue participating in catalysis. Method devlopment to specifically measure the active site cysteine pKa without interference from other cysteines, overview. As the magnitude of burst kinetics represents the amount of NADPH formed during the first turnover, it is directly dependent on the amount of the deprotonated form of cysteine. The pKa of Cys289 was calculated from a plot of the burst magnitude vs. pH as 7.4. The Cys289 pKa is also measured based on the ability of AbSSADH to form an NADP-cysteine adduct, which can be detected by the increase of absorbance at about 330 nm as 7.9. The lowering of the catalytic cysteine pKa by 0.6-1.0 unit renders the catalytic thiol more nucleophilic, which facilitates AbSSADH catalysis under physiological conditions. Deprotonation of the ligand or an active site residue is required for the SSADH reaction
additional information
the catalytic active center harbors residues such as Cys262, Glu228, Asn131, Arg139 and Ser420. Structure homology modeling of ApSSADH based on the crystal structure of enzyme SpSSADH (PDB ID 3VZ3) from Synechocystis sp. PCC6803. The residues of Cys262 and Asn131 interact with the carbonyl oxygen atom of SSA through the backbone NH group via hydrogen bond. Meanwhile, the side chains of Ser420 and Arg139 interact with the carboxyl oxygen of SSA directly. In addition, the side chains of Arg139 and Glu228 residues interact with the amide group of NADP+
additional information
the crystal structure with the bound product succinate shows that its carboxylate group establishes salt bridges with both Arg121 and Arg457, and a hydrogen bond with Tyr296. While both arginine residues are pre-formed for substrate/product binding, Tyr296 moves by more than 1.0 A. Key role of R121 and R457 residues in catalysis. Structure-function analysis, overview
additional information
-
the crystal structure with the bound product succinate shows that its carboxylate group establishes salt bridges with both Arg121 and Arg457, and a hydrogen bond with Tyr296. While both arginine residues are pre-formed for substrate/product binding, Tyr296 moves by more than 1.0 A. Key role of R121 and R457 residues in catalysis. Structure-function analysis, overview
additional information
-
structure analysis of the enzyme in binary and ternary with NADP(H) and/or substrate reveals that the enzyme forms a distinct reaction intermediate in each complex: a covalent adduct of a cofactor with the catalytic cysteine in the binary complex and a proposed thiohemiacetal intermediate in the ternary complex. SySSADH produces succinate in an NADP+ -dependent manner with a single cysteine acting as the catalytic residue in the catalytic loop, catalytic mechanism, overview. The formation of the NADP-cysteine adduct is a kinetically preferred event that protects the catalytic cysteine from H2O2-dependent oxidative stress. SySSADH shows a cofactor-dependent oxidation protection in 1-Cys SSADH, which is unique relative to other 2-Cys SSADHs employing a redox-dependent formation of a disulfide bridge. The catalytic cysteine preferentially forms an NADP-cysteine adduct if NADP+ is present
-
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in complex with NADP+, hanging drop vapour diffusion method, using 0.2 M ammonium tartrate, 26-31% polyethylene glycol 3350, 10 mM beta-mercaptoethanol and 0.1 M Tris (pH 7.2-7.5)
to 1.4 A resolution. The overall structure of SSADH shares the general fold of ALDH classes 1 and 2. The SSADH monomer is composed of three domains; an N-terminal NAD(P)-binding domain of residues 1125, 148256, and 457472, a catalytic domain of residues 257456, and an oligomerization domain of residues 126147 and 473482. The catalytic loop of Escherichia coli SSADH, unlike that of human SSADH, does not undergo disulfide bond-mediated structural changes upon changes of environmental redox status. The protein is not regulated via redox-switch modulation. A difference in the conformation of the connecting loop beta15beta16 causes the formation of a water molecule-mediated hydrogen bond network between the connecting loop and the catalytic loop in Escherichia coli SSADH
-
comparison to human enzyme, analysis of NADP+ binding site. Enzyme is a homotetramer with the 4 monomers related by a non-crystallographic 222 symmetry. The conserved catalytic site residues and active site residues correspond to C288 and E254 as well as R164, R282 and S445, respectively
purified PpALDH21 in apoform, and in complex with succinate and NADP+, X-ray diffraction structure determination and analysis at 2.15-2.30 A resolution, structure modeling
enzyme SpSSADH in a binary complex with succinate semialdehyde as the substrate and a ternary complex with succinate semialdehyde and NADP+, hanging-drop vapor diffusion method, mixing of mixture of 0.001 ml of protein solution with 0.001 ml of reservoir solution, for the binary complex crystal, SpSSADH is pre-incubated with succinate semialdehyde at the molar ratio of 1:2, and the protein-substrate mixture is crystallized over 00.5 ml of reservoir solution containing 0.1 M sodium acetate trihydrate, pH 4.6, and 2.0 M ammonium sulfate, the trinary complex is obtained by soaking the pre-grown NADP+ co-crystallized crystal with a 1:10 molar ratio of succinate semialdehyde under the same reservoir conditions, 22°C, X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacement method with the apo-structure of SpSSADH, PDB ID 4OGD, as the search model
structures in a binary complex with succinic semialdehyde as the substrate and a ternary complex with the substrate succinic semialdehyde and the inhibitory succinate semialdehyde, at 2.4 A resolution for both structures
structures in apo-form and in a binary complex with NADP+ at 1.6 A and 2.1 A resolutions, respectively. Both structures show dimeric conformation and contain a single cysteine residue in the catalytic loop of each subunit. Residues Ser158 and Tyr188 participate in the stabilization of the 2'-phosphate group of adenine-side ribose in NADP+
crystal structures of SySSADH determined in their apo form, as a binary complex with NADP+ and as a ternary complex with succinic semialdehyde and NADPH, resoultion of 1.7 A for the apo form and of 1.4 A for the binary and ternary complex
crystal structures of wild type Sp2771 at 2.1 A resolution, Sp2771 S419A mutant at 2.5 A resolution and ternary structure of non-catalytic Sp2771 C262A mutant in complex with NADP + and succinate semialdehyde at 1.7 A resolution
purified recombinant enzyme in apo form, in a binary complex with NADP+, and in a ternary complex with succinic semialdehyde and NADPH, sitting drop vapor diffusion method, using a crystallization buffer of 0.05 M potassium phosphate monobasic, 20% w/v PEG 8000, and 2 mM CaCl2, 22°C, for the binary and tertiary complexes, a pre-grown crystals of SySSADH are soaked for 60 min in a solution of 0.05 M potassium phosphate monobasic, 20% w/v PEG8000, 30% v/v ethylene glycol, and 50 mM NADPH or 50 mM NADPH and 50 mM succinate semialdehyde, respectively, X-ray diffraction structure determination and analysis at 1.4-1.7 A resolution, single-wavelength diffraction, modelling
purified recombinant His6-tagged wild-type Sp2771, and Sp2771 S419A and Sp2771 C262A mutants in ternary complex with NADP+ and succinate semialdehyde, mixing of 0.001 ml of protein solution and reservoir solution each, the latter containing 15% PEG 5000 MME , 1 mM DTT, 3% tascimate, and 100 mM HEPES, pH 6.8 for the wild-type enzyme and the mutants, for Sp2771 mutants in complex with NADP+ and succinate semialdehyde, NAD+ and succinate semialdehyde are incubated with proteins for 15 min at room temperature before crystallization, 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.7-2.5 A resolution, molecular replacement using Escherichia coli SSADH structure, PDB ID 3JZ4, as search model
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C289A
site-directed mutagenesis, inactive mutant
C291A
site-directed mutagenesis, the mutant shows 65% activity compared to wild-type enzyme
E228A
site-directed mutagenesis, inactive mutant
E228D
sitedirected mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme
N131A
site-directed mutagenesis, inactive mutant
N131D
site-directed mutagenesis, inactive mutant
R139A
site-directed mutagenesis, the mutant displays catalytic efficiency (kcat/Km) of only respective 0.2% compared to wild-type enzyme with significantly decreased binding affinity for succinic semialdehyde
S157E
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type, preferring NAD+, mutation of Ser157 does not significantly affect the binding affinity of SSA with the enzyme
S157P
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type, preferring NAD+, mutation of Ser157 does not significantly affect the binding affinity of SSA with the enzyme
S420A
site-directed mutagenesis, the mutant displays catalytic efficiency (kcat/Km) of only respective 0.4% compared to wild-type enzyme with significantly decreased binding affinity for succinic semialdehyde
N175A
site-directed mutagenesis, the mutant shows reduced activity compared tow wild-type enzyme
R121A
site-directed mutagenesis, almost inactive mutant
R228A
site-directed mutagenesis, the mutation results in 37fold lower catalytic efficiency value (kcat/Km) for NADP+, but only fourfold lower value for NAD+ compared to wild-type
R457A
site-directed mutagenesis, almost inactive mutant
Y296A
site-directed mutagenesis, the mutant shows reduced activity compared tow wild-type enzyme
E228Q
active site mutation, nonfunctional because Glu-228 acts as a general base
F132A
activity of about 1030% of the wild type enzyme, indicating a contribution of these succinic semialdehyde binding residues to the overall enzyme activity
F425A
inactive, suggesting that Phe-425 plays an important role in substrate binding
I263A
activity of about 1030% of the wild type enzyme, indicating a contribution of these succinic semialdehyde binding residues to the overall enzyme activity
N131A
mutation of a residue that interacts with the O4 atom or the carboxyl group of succinic semialdehyde thus abolishing enzyme activity
N131D
mutation of a residue that interacts with the O4 atom or the carboxyl group of succinic semialdehyde thus abolishing enzyme activity
R139K
mutant enzyme exhibited an activity up to 80% that of the wild type enzyme, suggesting the significance of a positively charged residue in the binding of the carboxyl group of succinic semialdehyde
S157E
mutation changes cofactor preference from NADP+ to NAD+, but enzyme activity is approximately 10fold reduced
W135A
activity of about 1030% of the wild type enzyme, indicating a contribution of these succinic semialdehyde binding residues to the overall enzyme activity
C262A
site-directed mutagenesis, Sp2771 mutant structure analysis and comparison to the wild-type structure
S419A
site-directed mutagenesis, Sp2771 mutant structure analysis and comparison to the wild-type structure
additional information
metabolic engineering of Corynebacterium glutamicum for the production of glutaric acid, a C5 dicarboxylic acid platform chemical, by co-expression of Pseudomonas putida davT, davB, and davD genes encoding lysine 2-monooxygenase, delta-aminovaleramidase, and glutarate semialdehyde dehydrogenase, respectively, in Corynebacterium glutamicum. Method optimization and evaluation. The glutaric acid biosynthesis pathway constructed in recombinant Corynebacterium glutamicum is engineered by examining strong synthetic promoters H30 and H36, Corynebacterium glutamicum codon-optimized davTDBA genes, and modification of davB gene with an N-terminal His6-tag to improve the production of glutaric acid. The use of N-terminal His6-tagged DavB is most suitable for the production of glutaric acid from glucose. Fed-batch fermentation of the final engineered Corynebacterium glutamicum H30_GAHis strain, expressing davTDA genes along with davB fused with His6-tag at N-terminus can produce 24.5 g/l of glutaric acid with low accumulation of L-lysine (1.7 g/l), wherein 5-aminovaleric acid (5-AVA) ccumulation is not observed during fermentation. Metabolically engineered Corynebacterium glutamicum strain KCTC H30_GA-2 (engineered strain KCTC 1857) is able for catalysis of the biosynthesis of glutaric acid from glucose. Method optimization and evaluation, overview
C262A
active site mutation, nonfunctional because Cys-262 acts as a nucleophilel
C262A
mutation abolishes catalytic activity, catalytic residue
E228A
active site mutation, nonfunctional because Glu-228 acts as a general base
E228A
mutation abolishes catalytic activity, catalytic residue
R139A
90% reduced catalytic activity, residue is involved in substrate binding
R139A
activity of about 1030% of the wild type enzyme, indicating a contribution of these succinic semialdehyde binding residues to the overall enzyme activity
S419A
80% reduced catalytic activity, residue is involved in substrate binding
S419A
mutation of a residue that interacts with the O4 atom or the carboxyl group of succinic semialdehyde thus abolishing enzyme activity
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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
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
Lutke-Eversloh, T.; Steinbuchel, A.
Biochemical and molecular characterization of a succinate semialdehyde dehydrogenase involved in the catabolism of 4-hydroxybutyric acid in Ralstonia eutropha
FEMS Microbiol. Lett.
181
63-71
1999
Cupriavidus necator (Q9RBF6)
brenda
Jaeger, M.; Rothacker, B.; Ilg, T.
Saturation transfer difference NMR studies on substrates and inhibitors of succinic semialdehyde dehydrogenases
Biochem. Biophys. Res. Commun.
372
400-406
2008
Escherichia coli (P25526)
brenda
Ahn, J.-W.; Kim, Y.-G.; Kim, K.-J.
Crystal structure of non-redox regulated SSADH from Escherichia coli
Biochem. Biophys. Res. Commun.
392
106-111
2010
Escherichia coli
brenda
Cozzani, I.; Fazio, A.M.; Felici, E.; Barletta, G.
Separation and characterization of NAD- and NADP-specific succinate-semialdehyde dehydrogenase from Escherichia coli K-12 3300
Biochim. Biophys. Acta
613
309-317
1980
Escherichia coli K-12
brenda
Sanchez, M.; Alvarez, M.A.; Balana, R.; Garrido-Pertierra, A.
Properties and functions of two succinic-semialdehyde dehydrogenases from Pseudomonas putida
Biochim. Biophys. Acta
953
249-257
1988
Pseudomonas putida
brenda
Bartsch, K.; von Johnn-Marteville, A.; Schulz, A.
Molecular analysis of two genes of the Escherichia coli gab cluster: nucleotide sequence of the glutamate:succinic semialdehyde transaminase gene (gabT) and characterization of the succinic semialdehyde dehydrogenase gene (gabD)
J. Bacteriol.
172
7035-7042
1990
Escherichia coli
brenda
Langendorf, C.G.; Key, T.L.; Fenalti, G.; Kan, W.T.; Buckle, A.M.; Caradoc-Davies, T.; Tuck, K.L.; Law, R.H.; Whisstock, J.C.
The X-ray crystal structure of Escherichia coli succinic semialdehyde dehydrogenase; structural insights into NADP+/enzyme interactions
PLoS One
5
e9280
2010
Escherichia coli (P25526), Escherichia coli K-12 (P25526), Escherichia coli MC1061 (P25526)
brenda
Esser, D.; Kouril, T.; Talfournier, F.; Polkowska, J.; Schrader, T.; Brsen, C.; Siebers, B.
Unraveling the function of paralogs of the aldehyde dehydrogenase super family from Sulfolobus solfataricus
Extremophiles
17
205-216
2013
Saccharolobus solfataricus (Q97XA5), Saccharolobus solfataricus P2 (Q97XA5)
brenda
de Carvalho, L.P.; Ling, Y.; Shen, C.; Warren, J.D.; Rhee, K.Y.
On the chemical mechanism of succinic semialdehyde dehydrogenase (GabD1) from Mycobacterium tuberculosis
Arch. Biochem. Biophys.
509
90-99
2011
Mycobacterium tuberculosis (P9WNX9), Mycobacterium tuberculosis H37Rv (P9WNX9)
brenda
Park, J.; Rhee, S.
Structural basis for a cofactor-dependent oxidation protection and catalysis of cyanobacterial succinic semialdehyde dehydrogenase
J. Biol. Chem.
288
15760-15770
2013
Synechococcus sp. (B1XMM6)
brenda
Yuan, Z.; Yin, B.; Wei, D.; Yuan, Y.R.
Structural basis for cofactor and substrate selection by cyanobacterium succinic semialdehyde dehydrogenase
J. Struct. Biol.
182
125-135
2013
Synechococcus sp. (B1XMM6)
brenda
Jang, E.H.; Park, S.A.; Chi, Y.M.; Lee, K.S.
Structural insight into the substrate inhibition mechanism of NADP(+)-dependent succinic semialdehyde dehydrogenase from Streptococcus pyogenes
Biochem. Biophys. Res. Commun.
461
487-493
2015
Streptococcus pyogenes (A0A0J9X1M8), Streptococcus pyogenes MGAS1882 (A0A0J9X1M8)
brenda
Jang, E.H.; Park, S.A.; Chi, Y.M.; Lee, K.S.
Kinetic and structural characterization for cofactor preference of succinic semialdehyde dehydrogenase from Streptococcus pyogenes
Mol. Cells
37
719-726
2014
Streptococcus pyogenes (A0A0J9X1M8), Streptococcus pyogenes MGAS1882 (A0A0J9X1M8)
brenda
Jang, E.H.; Park, S.A.; Chi, Y.M.; Lee, K.S.
Structural insight into the substrate inhibition mechanism of NADP+-dependent succinic semialdehyde dehydrogenase from Streptococcus pyogenes
Biochem. Biophys. Res. Commun.
461
487-493
2015
Streptococcus pyogenes (A0A0J9X1M8), Streptococcus pyogenes MG-AS1882 (A0A0J9X1M8)
brenda
Park, J.; Rhee, S.
Structural basis for a cofactor-dependent oxidation protection and catalysis of cyanobacterial succinic semialdehyde dehydrogenase
J. Biol. Chem.
288
15760-15770
2013
Synechococcus sp. (B1XMM6), Synechococcus sp. ATCC 27264 (B1XMM6)
brenda
Yuan, Z.; Yin, B.; Wei, D.; Yuan, Y.R.
Structural basis for cofactor and substrate selection by cyanobacterium succinic semialdehyde dehydrogenase
J. Struct. Biol.
182
125-135
2013
Synechococcus sp. PCC 7002 (B1XMM6)
brenda
Kim, H.T.; Khang, T.U.; Baritugo, K.A.; Hyun, S.M.; Kang, K.H.; Jung, S.H.; Song, B.K.; Park, K.; Oh, M.K.; Kim, G.B.; Kim, H.U.; Lee, S.Y.; Park, S.J.; Joo, J.C.
Metabolic engineering of Corynebacterium glutamicum for the production of glutaric acid, a C5 dicarboxylic acid platform chemical
Metab. Eng.
51
99-109
2019
Corynebacterium glutamicum (A0A1Q6BLU5)
brenda
Ito, S.; Osanai, T.
Unconventional biochemical regulation of the oxidative pentose phosphate pathway in the model cyanobacterium Synechocystis sp. PCC 6803
Biochem. J.
477
1309-1321
2020
Synechocystis sp. PCC 6803 (Q55585), Synechocystis sp. PCC 6803
brenda
Phonbuppha, J.; Maenpuen, S.; Munkajohnpong, P.; Chaiyen, P.; Tinikul, R.
Selective determination of the catalytic cysteine pKa of two-cysteine succinic semialdehyde dehydrogenase from Acinetobacter baumannii using burst kinetics and enzyme adduct formation
FEBS J.
285
2504-2519
2018
Acinetobacter baumannii (A0A0D5YDF1), Acinetobacter baumannii
brenda
Wang, X.; Lai, C.; Lei, G.; Wang, F.; Long, H.; Wu, X.; Chen, J.; Huo, G.; Li, Z.
Kinetic characterization and structural modeling of an NADP+-dependent succinic semialdehyde dehydrogenase from Anabaena sp. PCC7120
Int. J. Biol. Macromol.
108
615-624
2018
Nostoc sp. PCC 7120 = FACHB-418 (Q8YR92)
brenda
Kopecna, M.; Vigouroux, A.; Vilim, J.; Koncitikova, R.; Briozzo, P.; Hajkova, E.; Jaskova, L.; von Schwartzenberg, K.; Sebela, M.; Morera, S.; Kopecny, D.
The ALDH21 gene found in lower plants and some vascular plants codes for a NADP+-dependent succinic semialdehyde dehydrogenase
Plant J.
92
229-243
2017
Physcomitrium patens (A9SS48), Physcomitrium patens
brenda