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Literature summary for 1.2.1.79 extracted from

  • 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 (2011), Arch. Biochem. Biophys., 509, 90-99.
    View publication on PubMedView publication on EuropePMC

Inhibitors

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 [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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WNX9
-
-
Mycobacterium tuberculosis H37Rv P9WNX9
-
-

Oxidation Stability

Oxidation Stability Organism
GabD1 is naturally resistant to oxidation by H2O2 Mycobacterium tuberculosis

Substrates and Products (Substrate)

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

Synonyms Comment Organism
GabD1
-
Mycobacterium tuberculosis

Turnover Number [1/s]

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 Range

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

Cofactor Comment Organism Structure
NAD+ long incubations lead to modest utilization Mycobacterium tuberculosis
NADP+ preferred substrate Mycobacterium tuberculosis

Ki Value [mM]

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

General Information Comment Organism
metabolism enzyme catalyzes the last step of the gamma-aminobutyrate degradation Mycobacterium tuberculosis

kcat/KM [mM/s]

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