Evolutionarily distinct versions of the multidomain enzyme α-isopropylmalate synthase share discrete mechanisms of V-type allosteric regulation

Biochemistry

Volumn 53, Issue 29, 2014, Pages 4847-4856

  Kumar, Garima ^a   Frantom, Patrick A ^a  

^a UNIVERSITY OF ALABAMA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS;

ALLOSTERIC MECHANISMS; ALLOSTERIC REGULATION; FEEDBACK REGULATION; METHANOCOCCUS JANNASCHII; MULTI-DOMAIN ENZYMES; MYCOBACTERIUM TUBERCULOSIS; REGULATORY MECHANISM; STRUCTURE-FUNCTION RELATIONSHIP;

ENZYMES;

2 ISOPROPYLMALATE SYNTHASE; LEUCINE; LYASE; BACTERIAL PROTEIN;

ALLOSTERISM; AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; EVOLUTION; FEEDBACK SYSTEM; METHANOCALDOCOCCUS JANNASCHII; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; REGULATORY MECHANISM; ANTAGONISTS AND INHIBITORS; BIOCATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; KINETICS; METHANOCALDOCOCCUS; MOLECULAR EVOLUTION; PH; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SPECIES DIFFERENCE;

2-ISOPROPYLMALATE SYNTHASE; ALLOSTERIC REGULATION; BACTERIAL PROTEINS; BIOCATALYSIS; EVOLUTION, MOLECULAR; HYDROGEN-ION CONCENTRATION; KINETICS; LEUCINE; METHANOCALDOCOCCUS; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SPECIES SPECIFICITY;

EID: 84904976574     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500702u     Document Type: Article

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