Molecular basis of the substrate specificity and the catalytic mechanism of citramalate synthase from Leptospira interrogans

Biochemical Journal

Volumn 415, Issue 1, 2008, Pages 45-56

  Ma, Jun ^a,c   Zhang, Peng ^b,c   Zhang, Zilong ^a,c   Zha, Manwu ^b   Xu, Hai ^a,d   Zhao, Guoping ^a,e   Ding, Jianping ^b  

^a INSTITUTE OF PLANT PHYSIOLOGY AND ECOLOGY   (China)

^b INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^c UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^d SHANDONG UNIVERSITY   (China)

^e CHINESE NATIONAL HUMAN GENOME CENTER AT SHANGHAI   (China)

Author keywords

Aldol condensation; Catalytic mechanism; Citramalate synthase; Crystal structure; Feedback inhibition; Substrate specificity

Indexed keywords

ACIDS; AGENTS; CRYSTAL STRUCTURE; ENZYMES; MECHANISMS; PORT TERMINALS; POWDERS; TECHNOLOGICAL FORECASTING; THERMAL INSULATING MATERIALS;

ALDOL CONDENSATION; CATALYTIC MECHANISM; CITRAMALATE SYNTHASE; FEEDBACK INHIBITION; SUBSTRATE SPECIFICITY;

SUBSTRATES;

ANTIINFECTIVE AGENT; ARGININE; CITRAMALATE SYNTHASE; ENZYME; GLUTAMIC ACID; ISOLEUCINE; METHYL GROUP; PYRUVIC ACID; UNCLASSIFIED DRUG; (R) CITRAMALATE SYNTHASE; (R)-CITRAMALATE SYNTHASE; ACYLTRANSFERASE; MALONIC ACID; MALONIC ACID DERIVATIVE;

ALDOL REACTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; LEPTOSPIRA INTERROGANS; LEPTOSPIROSIS; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; ZOONOSIS; AMINO ACID SEQUENCE; BINDING SITE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CRYSTALLIZATION; ENZYMOLOGY; KINETICS; METABOLISM; MOLECULAR GENETICS; X RAY DIFFRACTION;

LEPTOSPIRA INTERROGANS;

ACYLTRANSFERASES; AMINO ACID SEQUENCE; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLIZATION; KINETICS; LEPTOSPIRA INTERROGANS; MALONATES; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; SUBSTRATE SPECIFICITY; X-RAY DIFFRACTION;

EID: 53149107492     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20080242     Document Type: Article

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