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Literature summary 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

EC Number Inhibitors Comment Organism Structure
1.2.1.16 additional information the enzyme is not influenced by 5 mM EDTA Mycobacterium tuberculosis
1.2.1.16 succinate semialdehyde
-
 Mycobacterium tuberculosis
1.2.1.79 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.16 0.003
-
 succinate semialdehyde with NADP+ as cosubstrate, in the presence of 10 mM Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.16 0.0092
-
 NAD+ in the presence of 10 mM Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.16 0.0133
-
 succinate semialdehyde with NADP+ as cosubstrate, in the absence of Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.16 0.0613
-
 NADP+ in the absence of Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.79 0.003
-
 Succinic semialdehyde steady-state parameter, 200 microM succinic semialdehyde and 10 mM Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.79 0.0092
-
 NADP+ steady-state parameter, 50 microM NADP+ and 10 mM Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.79 0.0133
-
 Succinic semialdehyde steady-state parameter, 200 microM succinic semialdehyde, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.79 0.0613
-
 NADP+ steady-state parameter, 50 microM NADP+, at pH 7.5 and 37°C Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.1.16 Ca2+
-
 Mycobacterium tuberculosis
1.2.1.16 Co2+
-
 Mycobacterium tuberculosis
1.2.1.16 Mg2+ 100% activity at 10 mM Mg2+. With Mg2+ there is a 4fold decrease in the Km value for succinate semialdehyde and a 6fold decrease in the Km value for NADP+ Mycobacterium tuberculosis
1.2.1.16 Mn2+
-
 Mycobacterium tuberculosis
1.2.1.16 additional information not activated by Cd2+ and Zn2+ Mycobacterium tuberculosis
1.2.1.16 Ni2+
-
 Mycobacterium tuberculosis
1.2.1.79 Ca2+ 2 to 3-fold activation at saturating concentration Mycobacterium tuberculosis
1.2.1.79 Co2+ 2 to 3-fold activation at saturating concentration Mycobacterium tuberculosis
1.2.1.79 Mg2+ 2 to 3-fold activation at saturating concentration Mycobacterium tuberculosis
1.2.1.79 Mn2+ 2 to 3-fold activation at saturating concentration Mycobacterium tuberculosis
1.2.1.79 additional information no activation with Cd2+ or Zn2+ Mycobacterium tuberculosis
1.2.1.79 Ni2+ 2 to 3-fold activation at saturating concentration Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.16 additional information Mycobacterium tuberculosis other aldehydes, such as formaldehyde, acetaldehyde and glutaraldehyde, are very poor substrates ?
-
 ?
1.2.1.16 succinate semialdehyde + NAD+ + H2O Mycobacterium tuberculosis
-
 succinate + NADH + H+
-
 ?
1.2.1.16 succinate semialdehyde + NADP+ + H2O Mycobacterium tuberculosis
-
 succinate + NADPH + H+
-
 ?
1.2.1.79 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
1.2.1.79 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

EC Number Organism UniProt Comment Textmining
1.2.1.16 Mycobacterium tuberculosis
-
-
-
1.2.1.79 Mycobacterium tuberculosis P9WNX9
-
-
1.2.1.79 Mycobacterium tuberculosis H37Rv P9WNX9
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.2.1.16 there is no significant loss of catalytic activity, after up to 40 min of incubation of isoform GabD1 with 1 mM H2O2 at pH 7.4 Mycobacterium tuberculosis
1.2.1.79 GabD1 is naturally resistant to oxidation by H2O2 Mycobacterium tuberculosis

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.16 Ni-NTA resin column chromatography Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.16 additional information other aldehydes, such as formaldehyde, acetaldehyde and glutaraldehyde, are very poor substrates Mycobacterium tuberculosis ?
-
 ?
1.2.1.16 succinate semialdehyde + NAD+ + H2O
-
 Mycobacterium tuberculosis succinate + NADH + H+
-
 ?
1.2.1.16 succinate semialdehyde + NADP+ + H2O
-
 Mycobacterium tuberculosis succinate + NADPH + H+
-
 ?
1.2.1.79 additional information other aldehydes, such as formaldehyde, acetaldehyde and glutaraldehyde, are very poor substrates showing a narrow substrate specificity of GabD1 Mycobacterium tuberculosis ?
-
 ?
1.2.1.79 additional information other aldehydes, such as formaldehyde, acetaldehyde and glutaraldehyde, are very poor substrates showing a narrow substrate specificity of GabD1 Mycobacterium tuberculosis H37Rv ?
-
 ?
1.2.1.79 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
1.2.1.79 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

EC Number Synonyms Comment Organism
1.2.1.16 GabD1 isoform Mycobacterium tuberculosis
1.2.1.16 succinic semialdehyde dehydrogenase
-
 Mycobacterium tuberculosis
1.2.1.79 GabD1
-
 Mycobacterium tuberculosis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.16 1.3
-
 NADP+ in the absence of Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.16 1.9
-
 succinate semialdehyde with NADP+ as cosubstrate, in the absence of Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.16 2.7
-
 NAD+ in the presence of 10 mM Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.16 4.7
-
 succinate semialdehyde with NADP+ as cosubstrate, in the presence of 10 mM Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.79 1.3
-
 NADP+ steady-state parameter, 50 microM NADP+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.79 1.9
-
 Succinic semialdehyde steady-state parameter, 200 microM succinic semialdehyde, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.79 2.7
-
 NADP+ steady-state parameter, 50 microM NADP+ and 10 mM Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.79 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

EC Number pH Minimum pH Maximum Comment Organism
1.2.1.16 5.5 10 the enzyme cannot be assayed below pH 5.5, due to precipitation and loss of activity Mycobacterium tuberculosis
1.2.1.79 5.5 10 GabD1 could not be assayed below pH 5.5, due to precipitation and loss of activity Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.16 NAD+ long incubations lead to a modest utilization of NAD+ as substrate Mycobacterium tuberculosis
1.2.1.16 NADP+ although long incubations lead to a modest utilization of NAD+ as substrate, NADP+ is the preferred substrate Mycobacterium tuberculosis
1.2.1.79 NAD+ long incubations lead to modest utilization Mycobacterium tuberculosis
1.2.1.79 NADP+ preferred substrate Mycobacterium tuberculosis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.2.1.16 0.0628
-
 succinate semialdehyde in the absence of Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.79 0.0628
-
 Succinic semialdehyde partial substrate inhibition, pH 7.5 and 37°C Mycobacterium tuberculosis

General Information

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

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.2.1.16 140
-
 succinate semialdehyde with NADP+ as cosubstrate, in the absence of Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.16 210
-
 NADP+ in the absence of Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.16 290
-
 NAD+ in the presence of 10 mM Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.16 1600
-
 succinate semialdehyde with NADP+ as cosubstrate, in the presence of 10 mM Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.79 21
-
 NADP+ steady-state parameter, 50 microM NADP+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.79 140
-
 Succinic semialdehyde steady-state parameter, 200 microM succinic semialdehyde, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.79 290
-
 NADP+ steady-state parameter, 50 microM NADP+ and 10 mM Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis
1.2.1.79 1600
-
 Succinic semialdehyde steady-state parameter, 200 microM succinic semialdehyde and 10 mM Mg2+, at pH 7.5 and 37°C Mycobacterium tuberculosis