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Literature summary extracted from

  • Park, S.A.; Park, Y.S.; Lee, K.S.
    Kinetic characterization and molecular modeling of NAD(P)+-dependent succinic semialdehyde dehydrogenase from Bacillus subtilis as an ortholog YneI (2014), J. Microbiol. Biotechnol., 24, 954-958 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.16 recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.16 succinate semialdehyde enzyme BsSSADH shows the substrate inhibition phenomenon in the presence of both NAD+ and NADP+ as cofactors at the concentration of succinate semialdehyde higher than 0.05 and 0.02 mM, respectively Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.16 additional information
-
 additional information Michaelis-Menten kinetics Bacillus subtilis
1.2.1.16 0.21
-
 NAD+ pH and temperature not specified in the publication Bacillus subtilis
1.2.1.16 0.39
-
 NADP+ pH and temperature not specified in the publication Bacillus subtilis
1.2.1.16 10.36
-
 succinate semialdehyde pH and temperature not specified in the publication, in presence of NAD+ Bacillus subtilis
1.2.1.16 20.5
-
 succinate semialdehyde pH and temperature not specified in the publication, in presence of NADP+ Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.16 succinate semialdehyde + NAD+ + H2O Bacillus subtilis
-
 succinate + NADH + 2 H+
-
 ?
1.2.1.16 succinate semialdehyde + NAD+ + H2O Bacillus subtilis 168
-
 succinate + NADH + 2 H+
-
 ?
1.2.1.16 succinate semialdehyde + NADP+ + H2O Bacillus subtilis
-
 succinate + NADPH + 2 H+
-
 ?
1.2.1.16 succinate semialdehyde + NADP+ + H2O Bacillus subtilis 168
-
 succinate + NADPH + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.16 Bacillus subtilis
-
-
-
1.2.1.16 Bacillus subtilis 168
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.16 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and gel filtration Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.16 succinate semialdehyde + NAD+ + H2O
-
 Bacillus subtilis succinate + NADH + 2 H+
-
 ?
1.2.1.16 succinate semialdehyde + NAD+ + H2O
-
 Bacillus subtilis 168 succinate + NADH + 2 H+
-
 ?
1.2.1.16 succinate semialdehyde + NADP+ + H2O
-
 Bacillus subtilis succinate + NADPH + 2 H+
-
 ?
1.2.1.16 succinate semialdehyde + NADP+ + H2O
-
 Bacillus subtilis 168 succinate + NADPH + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.16 More structure modeling Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
1.2.1.16 BsSSADH
-
 Bacillus subtilis
1.2.1.16 NAD(P)+-dependent succinic semialdehyde dehydrogenase
-
 Bacillus subtilis
1.2.1.16 SSADH
-
 Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.16 5.26
-
 NAD+ pH and temperature not specified in the publication Bacillus subtilis
1.2.1.16 5.61
-
 succinate semialdehyde pH and temperature not specified in the publication, in presence of NAD+ Bacillus subtilis
1.2.1.16 7.24
-
 succinate semialdehyde pH and temperature not specified in the publication, in presence of NADP+ Bacillus subtilis
1.2.1.16 9.93
-
 NADP+ pH and temperature not specified in the publication Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.16 additional information NAD(P)+-dependent succinic semialdehyde dehydrogenase, BsSSADH shows similar values of the catalytic efficiency (kcat/Km) in both NAD+ and NADP+ as cofactors. The affinity of enzyme BsSSADH to NAD+ is approximately 2fold higher than that to NADP+, but the values of kcat are almost 2fold higher in the presence of NADP+ than NAD+ Bacillus subtilis
1.2.1.16 NAD+
-
 Bacillus subtilis
1.2.1.16 NADP+
-
 Bacillus subtilis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.2.1.16 28.3
-
 succinate semialdehyde pH and temperature not specified in the publication, in presence of NADP+ Bacillus subtilis
1.2.1.16 470.6
-
 succinate semialdehyde pH and temperature not specified in the publication, in presence of NAD+ Bacillus subtilis

General Information

EC Number General Information Comment Organism
1.2.1.16 metabolism succinic semialdehyde dehydrogenase (SSADH) catalyzes the oxidation of succinic semialdehyde (SSA) into succinic acid in the final step of gamma-aminobutyric acid degradation Bacillus subtilis

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 0.362
-
 succinate semialdehyde pH and temperature not specified in the publication, in presence of NADP+ Bacillus subtilis
1.2.1.16 0.598
-
 succinate semialdehyde pH and temperature not specified in the publication, in presence of NAD+ Bacillus subtilis
1.2.1.16 25.1
-
 NAD+ pH and temperature not specified in the publication Bacillus subtilis
1.2.1.16 25.4
-
 NADP+ pH and temperature not specified in the publication Bacillus subtilis