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Literature summary for 1.2.1.27 extracted from

  • Stines-Chaumeil, C.; Talfournier, F.; Branlant, G.
    Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis (2006), Biochem. J., 395, 107-115.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.1.27

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
C49A/C176A/C305A/C369A/C403A kinetic parameters similar to the wild-type enzmye Bacillus subtilis
W177F NAD-binding followed by fluorescence quenching of methylmalonate semialdehyde dehydrogenase. Only W468 is responsible for time-dependent additional quenching Bacillus subtilis
W28F NAD-binding followed by fluorescence quenching of methylmalonate semialdehyde dehydrogenase. Only W468 is responsible for time-dependent additional quenching Bacillus subtilis
W397F NAD-binding followed by fluorescence quenching of methylmalonate semialdehyde dehydrogenase. Only W468 is responsible for time-dependent additional quenching Bacillus subtilis
W468F NAD-binding followed by fluorescence quenching of methylmalonate semialdehyde dehydrogenase. Only W468 is responsible for time-dependent additional quenching Bacillus subtilis
W76F NAD-binding followed by fluorescence quenching of methylmalonate semialdehyde dehydrogenase. Only W468 is responsible for time-dependent additional quenching Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.06
-
 2-Methyl-3-oxopropanoate 50 mM KP04 pH 8.2, 30°C, 0.5 mM 2-methyl-3-oxopropanoate, 12 mM NAD+, 0.5 mM CoA Bacillus subtilis
0.12
-
 CoA 50 mM potassium phosphate pH 8.2, 30°C, 0.5 mM 2-methyl-3-oxopropanoate, 12 mM NAD+, 0.5 mM CoA Bacillus subtilis
2.3
-
 NAD+ 50 mM potassium phosphate pH 8.2, 30°C, 0.5 mM 2-methyl-3-oxopropanoate, 12 mM NAD+, 0.5 mM CoA Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis

Source Tissue

Source Tissue Comment Organism Textmining
cell culture
-
 Bacillus subtilis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-methyl-3-oxopropanoate + CoA + NAD+
-
 Bacillus subtilis propanoyl-CoA + CO2 + NADH
-
 ?
malonate semialdehyde + CoA + NAD+
-
 Bacillus subtilis acetyl-CoA + CO2 + NADH
-
 ?

Synonyms

Synonyms Comment Organism
methylmalonate semialdehyde dehydrogenase
-
 Bacillus subtilis
MSDH
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
 Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1
-
 2-Methyl-3-oxopropanoate 50 mM potassium phosphate pH 8.2, 30°C, 0.5 mM 2-methyl-3-oxopropanoate, 12 mM NAD+, 0.5 mM CoA Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.2
-
-
 Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Bacillus subtilis