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Volumn 52, Issue 39, 2013, Pages 6737-6739

V -type allosteric inhibition is described by a shift in the rate-determining step for α-Isopropylmalate synthase from mycobacterium tuberculosis

(4) Casey, Ashley K a Schwalm, Erica L a Hays, Brittani N a Frantom, Patrick A a

a UNIVERSITY OF ALABAMA (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC INHIBITION; ALLOSTERIC MECHANISMS; KINETIC ISOTOPE EFFECTS; MYCOBACTERIUM TUBERCULOSIS; PRODUCT RELEASE; RATE DETERMINING STEP; RELATIVE RATES; SYNTHASES;

ISOTOPES; RATE CONSTANTS; REACTION KINETICS;

KINETICS;

2 ISOPROPYLMALATE SYNTHASE; LEUCINE;

ALLOSTERISM; ARTICLE; CATALYSIS; KINETICS; MYCOBACTERIUM TUBERCULOSIS; PRIORITY JOURNAL;

2-ISOPROPYLMALATE SYNTHASE; ALLOSTERIC REGULATION; AMINO ACIDS; BIOCATALYSIS; KINETICS; LEUCINE; MOLECULAR STRUCTURE; MYCOBACTERIUM TUBERCULOSIS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84885015070 PISSN: 00062960 EISSN: 15204995 Source Type: Journal
DOI: 10.1021/bi401186v Document Type: Article

Times cited : (11)

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