Methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis: Substrate specificity and coenzyme A binding

Journal of Biological Chemistry

Volumn 286, Issue 25, 2011, Pages 21971-21981

  Talfournier, François ^a   Stines Chaumeil, Claire ^a,b   Branlant, Guy ^a  

^a CNRS   (France)

^b Institut de Biochimie et Genetique Cellulaires   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLATION; ALDEHYDES; AMINO ACIDS; ARGININE; BACTERIOLOGY; BINDING SITES; CATALYSIS; ENZYMES; RATE CONSTANTS; SUBSTRATES;

ALDEHYDE DEHYDROGENASE; CARBOXYLATE GROUPS; CATALYTIC EFFICIENCIES; DECARBOXYLATION PROCESS; SECOND-ORDER RATE CONSTANTS; SEMIALDEHYDE DEHYDROGENASE; SUBSTRATE SPECIFICITY; TRANSTHIOESTERIFICATION;

CARBOXYLATION;

ARGININE; COENZYME A; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LEUCINE; METHYLMALONATE SEMIALDEHYDE DEHYDROGENASE (ACYLATING); PROPIONALDEHYDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

ACYLATION; AMINO ACID SUBSTITUTION; ARTICLE; BACILLUS SUBTILIS; BINDING AFFINITY; BINDING SITE; CATALYSIS; CONTROLLED STUDY; DEACETYLATION; ENZYME BINDING; ENZYME KINETICS; ENZYME MECHANISM; ENZYME RELEASE; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ESTERIFICATION; IONIC STRENGTH; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; STEADY STATE; STREPTOCOCCUS MUTANS;

BACILLUS SUBTILIS;

EID: 79959371622     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.213280     Document Type: Article

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