The roles of two amino acid residues in the active site of L-lactate monooxygenase. Mutation of arginine 187 to methionine and histidine 240 to glutamine

Journal of Biological Chemistry

Volumn 274, Issue 32, 1999, Pages 22289-22295

  Sanders, Stephen A ^a   Williams Jr , Charles H ^b   Massey, Vincent ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b VA ANN ARBOR HEALTHCARE SYSTEM   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ARGININE; GLUTAMINE; HISTIDINE; LACTATE 2 MONOOXYGENASE; LACTATE DEHYDROGENASE (CYTOCHROME); LACTIC ACID; PYRUVIC ACID; QUERCETIN;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CATALYSIS; DISSOCIATION CONSTANT; ENZYME ACTIVE SITE; ENZYME BINDING; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN FAMILY; THERMODYNAMICS;

ARGININE; CATALYTIC DOMAIN; HISTIDINE; HYDROGEN PEROXIDE; LACTIC ACID; METHYL METHANESULFONATE; MIXED FUNCTION OXYGENASES; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; OXALATES; OXIDATION-REDUCTION; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

ANIMALIA; FELIS CATUS; SACCHAROMYCES CEREVISIAE; STAPHYLOCOCCUS PHAGE 187;

EID: 0033529542     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.32.22289     Document Type: Article

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