The role of the active site glutamate in the rearrangement of glutamate to 3-methylaspartate catalyzed by adenosylcobalamin-dependent glutamate mutase

Chemistry and Biology

Volumn 8, Issue 12, 2001, Pages 1143-1149

  Madhavapeddi, Prashanti ^a   Marsh, E Neil G ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

Author keywords

Coenzyme B12; Enzyme; Free radical; Isotope effect; Mutagenesis

Indexed keywords

3 METHYLASPARTIC ACID; 3-METHYLASPARTIC ACID; ASPARTIC ACID; COBAMAMIDE; DRUG DERIVATIVE; GLUTAMIC ACID; METHYLASPARTATE MUTASE; MUTASE;

ARTICLE; BINDING SITE; CATALYSIS; CHEMISTRY; ENZYME SPECIFICITY; GENETICS; KINETICS; METABOLISM; MUTATION;

ASPARTIC ACID; BINDING SITES; CATALYSIS; COBAMIDES; GLUTAMIC ACID; INTRAMOLECULAR TRANSFERASES; KINETICS; MUTATION; SUBSTRATE SPECIFICITY; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0035542850     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(01)00081-3     Document Type: Article

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