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Literature summary extracted from

  • Talfournier, F.; Stines-Chaumeil, C.; Branlant, G.
    Methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis: substrate specificity and coenzyme A binding (2011), J. Biol. Chem., 286, 21971-21981.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.27 R124L results obtained under pre-steady conditions show that both Arg residues participate not only in methylmalonate semialdehyde binding via stabilizing interactions between the guanidinium groups and the carboxylate but also in the formation of an efficient MSDH-NAD+-methylmalonate semialdehyde ternary complex Bacillus subtilis
1.2.1.27 R301L results obtained under pre-steady conditions show that both Arg residues participate not only in methylmalonate semialdehyde binding via stabilizing interactions between the guanidinium groups and the carboxylate but also in the formation of an efficient MSDH-NAD+-methylmalonate semialdehyde ternary complex Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.27 additional information
-
 additional information Km-value of CoA for R301L mutant enzyme under steady-state conditions with propionaldehyde is above 1 mM at pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.006
-
 methylmalonate semialdehyde R124L mutant enzyme, steady-state conditions, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.023
-
 methylmalonate semialdehyde R301L mutant enzyme, steady-state conditions, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.033
-
 NAD+ wild type MSDH, steady-state conditions with propionaldehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.038
-
 NAD+ R124L mutant enzyme, steady-state conditions with propionaldehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.06
-
 NAD+ R124L mutant enzyme, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.06
-
 methylmalonate semialdehyde wild type MSDH, steady-state conditions, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.085
-
 CoA wild type MSDH, steady-state conditions with propionaldehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.12
-
 NAD+ R301L mutant enzyme, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.12
-
 CoA wild type MSDH, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.33
-
 CoA R124L mutant enzyme, steady-state conditions with propionaldehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.57
-
 CoA R124L mutant enzyme, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.62
-
 CoA R301L mutant enzyme, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 2.3
-
 NAD+ wild type MSDH, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 9.3
-
 propionaldehyde R124L mutant enzyme, steady-state conditions, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 9.8
-
 propionaldehyde wild type MSDH, steady-state conditions, pH 8.2 and 30°C Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.27 Bacillus subtilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.27 MSDH purified by ammonium sulfate fractionation, 40-80%, and gel filtration on a ACA 34 resin Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.27 methylmalonate semialdehyde + CoA + H2O + NAD+
-
 Bacillus subtilis propanoyl-CoA + HCO3- + NADH
-
 ?
1.2.1.27 propionaldehyde + CoA + NAD+
-
 Bacillus subtilis propanoyl-CoA + NADH
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.27 MSDH
-
 Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.27 additional information
-
 additional information Kcat-value of CoA for R301L mutant enzyme under steady-state conditions with propionaldehyde is above 3 1/sec at pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.06
-
 NAD+ R124L mutant enzyme, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.14
-
 NAD+ R301L mutant enzyme, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 2.2
-
 NAD+ wild type MSDH, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 2.8
-
 CoA R124L mutant enzyme, steady-state conditions with propionaldehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 12.6
-
 CoA wild type MSDH, steady-state conditions with propionaldehyde, pH 8.2 and 30°C Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.2.1.27 5 8.8
-
 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
1.2.1.27 3
-
 CoA R301L mutant enzyme, steady-state conditions with propionaldehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 8.5
-
 CoA R124L mutant enzyme, steady-state conditions with propionaldehyde, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 150
-
 CoA wild type MSDH, steady-state conditions with propionaldehyde, pH 8.2 and 30°C Bacillus subtilis