Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Bchini, R.; Dubourg-Gerecke, H.; Rahuel-Clermont, S.; Aubry, A.; Branlant, G.; Didierjean, C.; Talfournier, F.
    Adenine binding mode is a key factor in triggering the early release of NADH in coenzyme A-dependent methylmalonate semialdehyde dehydrogenase (2012), J. Biol. Chem., 287, 31095-31103.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.27 in Escherichia coli DH5[alpha] transformants containing the pSKmsdbsub plasmid Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.27 methylmalonate semialdehyde dehydrogenase in binary complex with NAD+, showing that the nicotinamide ring is well defined in the electron density due to direct and H2O-mediated hydrogen bonds with the carboxamide and that a conformational isomerization of the NMNH is possible in MSDH Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.27 additional information further mutant enzyme created by single insertion of glycine at position 225 resulting in significant decrease of the rate constant associated with the dissociation of NADH fromthe NADH/thioacylenzyme complex Bacillus subtilis
1.2.1.27 N427L substitution dramatically alters the catalytic properties of the enzyme, acylation becomes rate-limiting with a decrease of the associated rate constant by at least 10000fold relative to the wild-type MSDH Bacillus subtilis
1.2.1.27 V229G significant decrease of the rate constant associated with the dissociation of NADH from the NADH-thioacylenzyme complex Bacillus subtilis
1.2.1.27 V229G together with insertion of glycine at position 225, significant decrease of the rate constant associated with the dissociation of NADH from the NADH/thioacylenzyme complex Bacillus subtilis
1.2.1.27 V229G/H226P rate-limiting step changes to acylation instead of deacylation Bacillus subtilis
1.2.1.27 V229G/H226P together with insertion of glycine at position 225, rate-limiting step changes to acylation instead of deacylation Bacillus subtilis
1.2.1.27 V229G/Y252L/V253I together with insertion of glycine at position 225, rate-limiting step changes to acylation instead of deacylation Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.27 0.021
-
 methylmalonate semialdehyde V229G/H226P/G225 insertion, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.022
-
 methylmalonate semialdehyde G225 insertion, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.027
-
 methylmalonate semialdehyde V229G/G225 insertion, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.028
-
 methylmalonate semialdehyde V229G/H226P, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.054
-
 methylmalonate semialdehyde V229G, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.06
-
 methylmalonate semialdehyde wild type MSDH, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.063
-
 CoA V229G/G225 insertion, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.096
-
 CoA V229G/H226P/G225 insertion, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.119
-
 CoA V229G/H226P, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.12
-
 CoA wild type MSDH, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.15
-
 NAD+ V229G/G225 insertion, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.151
-
 CoA G225 insertion, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.215
-
 methylmalonate semialdehyde V229G/Y252L/V253I/G225 insertion, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.234
-
 CoA V229G, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.497
-
 CoA V229G/Y252L/V253I/G225 insertion, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.57
-
 NAD+ V229G, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.66
-
 NAD+ V229G/H226P, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.69
-
 NAD+ G225 insertion, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.77
-
 NAD+ V229G/H226P/G225 insertion, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 2.3
-
 NAD+ wild type MSDH, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 9.44
-
 NAD+ V229G/Y252L/V253I/G225 insertion, pH 8.2 and 30°C Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.27 Bacillus subtilis P42412
-
-

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+ weaker stabilization of the adenine ring triggers early NADH release in MSDH-catalyzed reaction Bacillus subtilis propanoyl-CoA + HCO3- + NADH
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.27 tetramer dimer of dimers, monomer consists of three domains, the dinucleotide binding domain comprising the residues 3–123 and 141–251, the catalytic domain with residues 252–270, and a small domain, with residues 124–140 and 471–486 Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
1.2.1.27 methylmalonate semialdehyde dehydrogenase
-
 Bacillus subtilis
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 0.02
-
 NAD+ V229G/H226P/G225 insertion, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.02
-
 NAD+ V229G/Y252L/V253I/G225 insertion, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.09
-
 NAD+ V229G/H226P, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.21
-
 NAD+ V229G/G225 insertion, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.39
-
 NAD+ G225 insertion, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 0.78
-
 NAD+ V229G, pH 8.2 and 30°C Bacillus subtilis
1.2.1.27 2.2
-
 NAD+ wild type MSDH, pH 8.2 and 30°C Bacillus subtilis