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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+
-
-
-
?
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+
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+
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 + 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
?
-
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+
-
-
-
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 + 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
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
additional information

no cofactor: NAD+
-
additional information
no detectable activity by using NAD+ as cofactor
-
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3-tolualdehyde
only the aldehyde forms and not the gem-diol forms of the inhibitor 3-tolualdehyde bind to the enzyme
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.01 mM, 29% residual activity
H2O2
50 microM H2O2 sharply reduces activity to 31% of the H2O2-free enzyme and activity further decreases to 3% at 1 mM H2O2
N-ethylmaleimide
-
0.1 mM, complete loss of activity
Succinic semialdehyde
partial substrate inhibition because velocity decreases to a non-zero value at saturating concentrations of Mg2+ and succinic semialdehyde
Zn2+
-
1 mM, complete inhibition
NADPH

-
-
succinate semialdehyde

-
substrate inhibition above 1 mM
succinate semialdehyde
uncompetitive substrate inhibition above 0.02 mM, in the presence of NADP+. Substrate inhibition is induced by the binding of inhibitory succinate semialdehyde in the cofactor-binding site, instead of NADP+
succinate semialdehyde
complete uncompetitive substrate inhibition. 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+
additional information

-
not inhibitory: succinate, pyruvate
-
additional information
-
not inhibitory: succinate, pyruvate
-
additional information
analysis of the kinetic inhibitory parameters revealed significant substrate inhibition in the presence of NADP+ at concentrations of succinate semialdehyde higher than 0.02 mM, which exhibits complete uncompetitive substrate inhibition, structure-based molecular insights into the substrate inhibition mechanism of SpSSADH, overview
-
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evolution

SSADH belongs to the aldehyde dehydrogenase (ALDH) superfamily
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
-
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
-
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
-
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 1â125, 148â256, and 457â472, a catalytic domain of residues 257â456, and an oligomerization domain of residues 126â147 and 473â482. 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 beta15âbeta16 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
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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E228Q
active site mutation, nonfunctional because Glu-228 acts as a general base
F132A
activity of about 10â30% 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 10â30% 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 10â30% 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
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 10â30% 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
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Escherichia coli K-12
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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)
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Escherichia coli (P25526), Escherichia coli K-12 (P25526), Escherichia coli MC1061 (P25526)
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Saccharolobus solfataricus (Q97XA5), Saccharolobus solfataricus P2 (Q97XA5)
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Mycobacterium tuberculosis (P9WNX9), Mycobacterium tuberculosis H37Rv (P9WNX9)
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Synechococcus sp. (B1XMM6)
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Synechococcus sp. (B1XMM6)
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Streptococcus pyogenes (A0A0J9X1M8), Streptococcus pyogenes MGAS1882 (A0A0J9X1M8)
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Streptococcus pyogenes (A0A0J9X1M8), Streptococcus pyogenes MGAS1882 (A0A0J9X1M8)
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Structural insight into the substrate inhibition mechanism of NADP+-dependent succinic semialdehyde dehydrogenase from Streptococcus pyogenes
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Streptococcus pyogenes (A0A0J9X1M8), Streptococcus pyogenes MG-AS1882 (A0A0J9X1M8)
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Park, J.; Rhee, S.
Structural basis for a cofactor-dependent oxidation protection and catalysis of cyanobacterial succinic semialdehyde dehydrogenase
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288
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Synechococcus sp. (B1XMM6), Synechococcus sp. ATCC 27264 (B1XMM6)
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Yuan, Z.; Yin, B.; Wei, D.; Yuan, Y.R.
Structural basis for cofactor and substrate selection by cyanobacterium succinic semialdehyde dehydrogenase
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182
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Synechococcus sp. PCC 7002 (B1XMM6)
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