The carboligation reaction of acetohydroxyacid synthase II: Steady-state intermediate distributions in wild type and mutants by NMR

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 3, 2005, Pages 553-558

  Tittmann, Kai ^b   Vyazmensky, Maria ^a   Hübner, Gerhard ^b   Barak, Ze'ev ^a   Chipman, David M ^a  

^a BEN GURION UNIVERSITY OF THE NEGEV   (Israel)

^b MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

Amino acid biosynthesis; Mechanism; Thiamin diphosphate

Indexed keywords

ACETOLACTATE SYNTHASE; BRANCHED CHAIN AMINO ACID; BUTYRIC ACID; COCARBOXYLASE; ENAMINE; ISOLEUCINE; LEUCINE; MUTANT PROTEIN; PYRUVIC ACID; VALINE;

AMINO ACID SYNTHESIS; ARTICLE; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SPECIFICITY; ESCHERICHIA COLI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; STEADY STATE; TURNOVER TIME; WILD TYPE;

ACETOLACTATE SYNTHASE; AMINO ACIDS, BRANCHED-CHAIN; BINDING SITES; CARBOXYLIC ACIDS; CONSERVED SEQUENCE; ESCHERICHIA COLI PROTEINS; KINETICS; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI;

EID: 14144249867     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0408210101     Document Type: Article

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