Reaction of serine-glyoxylate aminotransferase with the alternative substrate ketomalonate indicates rate-limiting protonation of a quinonoid intermediate

Biochemistry

Volumn 44, Issue 48, 2005, Pages 15930-15936

  Karsten, William E ^a   Ohshiro, Takashi ^b   Izumi, Yoshikazu ^b   Cook, Paul F ^a  

^a UNIVERSITY OF OKLAHOMA   (United States)

^b TOTTORI UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

DEUTERIUM; ENZYMES; ESTERS; ISOTOPES; PROTONS; REACTION KINETICS; SUBSTRATES;

GLYOXYLATE; ISOTOPE EFFECTS; PROTONATION; SERINE-GLYOXYLATE AMINOTRANSFERASE (SGAT);

ENZYME KINETICS;

AMINOTRANSFERASE; GLYCINE; GLYOXYLIC ACID DERIVATIVE; HYDROXYPYRUVIC ACID; KETOMALONATE; MALONIC ACID DERIVATIVE; PYRIDOXAL 5 PHOSPHATE; PYRUVIC ACID DERIVATIVE; QUINONE DERIVATIVE; SCHIFF BASE; SERINE; SERINE GLYOXYLATE AMINOTRANSFERASE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CHEMICAL REACTION KINETICS; HYPHOMICROBIUM; HYPHOMICROBIUM METHYLOVORUM; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; REACTION ANALYSIS; STEADY STATE;

DEUTERIUM; HYPHOMICROBIUM; KINETICS; MALONATES; QUINONES; SCHIFF BASES; SERINE; TRANSAMINASES;

HYPHOMICROBIUM; HYPHOMICROBIUM METHYLOVORUM;

EID: 28544439299     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051407p     Document Type: Article

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