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Volumn 519, Issue 2, 2012, Pages 202-209

Structural and functional characterization of α-isopropylmalate synthase and citramalate synthase, members of the LeuA dimer superfamily

(1) Frantom, Patrick A a

a UNIVERSITY OF ALABAMA (United States)

Author keywords

Allosteric regulation; Branched chain amino acid biosynthesis; Citramalate synthase; Hydrogen deuterium exchange; Isopropylmalate synthase; LeuA dimer domain

Indexed keywords

2 ISOPROPYLMALATE SYNTHASE; BACTERIAL ENZYME; CITRAMALATE SYNTHASE; DIMER; SYNTHETASE; UNCLASSIFIED DRUG;

ALLOSTERISM; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ISOLATION; ENZYME MECHANISM; ENZYME REGULATION; ENZYME STRUCTURE; LEPTOSPIRA INTERROGANS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; REVIEW; SALMONELLA TYPHIMURIUM;

2-ISOPROPYLMALATE SYNTHASE; ACETYLTRANSFERASES; ALLOSTERIC REGULATION; BACTERIA; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY;

EID: 84857829354 PISSN: 00039861 EISSN: 10960384 Source Type: Journal
DOI: 10.1016/j.abb.2011.10.009 Document Type: Review

Times cited : (18)

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