Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Succinic semialdehyde | partial substrate inhibition because velocity decreases to a non-zero value at saturating concentrations of Mg2+ and succinic semialdehyde | Mycobacterium tuberculosis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.003 | - |
Succinic semialdehyde | steady-state parameter, 200 microM succinic semialdehyde and 10 mM Mg2+, at pH 7.5 and 37°C | Mycobacterium tuberculosis | |
0.0092 | - |
NADP+ | steady-state parameter, 50 microM NADP+ and 10 mM Mg2+, at pH 7.5 and 37°C | Mycobacterium tuberculosis | |
0.0133 | - |
Succinic semialdehyde | steady-state parameter, 200 microM succinic semialdehyde, at pH 7.5 and 37°C | Mycobacterium tuberculosis | |
0.0613 | - |
NADP+ | steady-state parameter, 50 microM NADP+, at pH 7.5 and 37°C | Mycobacterium tuberculosis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | 2 to 3-fold activation at saturating concentration | Mycobacterium tuberculosis | |
Co2+ | 2 to 3-fold activation at saturating concentration | Mycobacterium tuberculosis | |
Mg2+ | 2 to 3-fold activation at saturating concentration | Mycobacterium tuberculosis | |
Mn2+ | 2 to 3-fold activation at saturating concentration | Mycobacterium tuberculosis | |
additional information | no activation with Cd2+ or Zn2+ | Mycobacterium tuberculosis | |
Ni2+ | 2 to 3-fold activation at saturating concentration | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
succinic semialdehyde + NADP+ + H2O | Mycobacterium tuberculosis | 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 | succinate + NADPH + 2 H+ | - |
ir | |
succinic semialdehyde + NADP+ + H2O | Mycobacterium tuberculosis H37Rv | 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 | succinate + NADPH + 2 H+ | - |
ir |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WNX9 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WNX9 | - |
- |
Oxidation Stability | Organism |
---|---|
GabD1 is naturally resistant to oxidation by H2O2 | Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | other aldehydes, such as formaldehyde, acetaldehyde and glutaraldehyde, are very poor substrates showing a narrow substrate specificity of GabD1 | Mycobacterium tuberculosis | ? | - |
? | |
additional information | other aldehydes, such as formaldehyde, acetaldehyde and glutaraldehyde, are very poor substrates showing a narrow substrate specificity of GabD1 | Mycobacterium tuberculosis H37Rv | ? | - |
? | |
succinic semialdehyde + NADP+ + H2O | 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 | Mycobacterium tuberculosis | succinate + NADPH + 2 H+ | - |
ir | |
succinic semialdehyde + NADP+ + H2O | 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 | Mycobacterium tuberculosis H37Rv | succinate + NADPH + 2 H+ | - |
ir |
Synonyms | Comment | Organism |
---|---|---|
GabD1 | - |
Mycobacterium tuberculosis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.3 | - |
NADP+ | steady-state parameter, 50 microM NADP+, at pH 7.5 and 37°C | Mycobacterium tuberculosis | |
1.9 | - |
Succinic semialdehyde | steady-state parameter, 200 microM succinic semialdehyde, at pH 7.5 and 37°C | Mycobacterium tuberculosis | |
2.7 | - |
NADP+ | steady-state parameter, 50 microM NADP+ and 10 mM Mg2+, at pH 7.5 and 37°C | Mycobacterium tuberculosis | |
4.7 | - |
Succinic semialdehyde | steady-state parameter, 200 microM succinic semialdehyde and 10 mM Mg2+, at pH 7.5 and 37°C | Mycobacterium tuberculosis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5.5 | 10 | GabD1 could not be assayed below pH 5.5, due to precipitation and loss of activity | Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | long incubations lead to modest utilization | Mycobacterium tuberculosis | |
NADP+ | preferred substrate | Mycobacterium tuberculosis |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0628 | - |
Succinic semialdehyde | partial substrate inhibition, pH 7.5 and 37°C | Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
metabolism | enzyme catalyzes the last step of the gamma-aminobutyrate degradation | Mycobacterium tuberculosis |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
21 | - |
NADP+ | steady-state parameter, 50 microM NADP+, at pH 7.5 and 37°C | Mycobacterium tuberculosis | |
140 | - |
Succinic semialdehyde | steady-state parameter, 200 microM succinic semialdehyde, at pH 7.5 and 37°C | Mycobacterium tuberculosis | |
290 | - |
NADP+ | steady-state parameter, 50 microM NADP+ and 10 mM Mg2+, at pH 7.5 and 37°C | Mycobacterium tuberculosis | |
1600 | - |
Succinic semialdehyde | steady-state parameter, 200 microM succinic semialdehyde and 10 mM Mg2+, at pH 7.5 and 37°C | Mycobacterium tuberculosis |