Amino-acid substitutions at the domain interface affect substrate and allosteric inhibitor binding in α-isopropylmalate synthase from Mycobacterium tuberculosis

Biochemical and Biophysical Research Communications

Volumn 433, Issue 2, 2013, Pages 249-254

  Huisman, Frances H A ^a   Squire, Christopher J ^b   Parker, Emily J ^a  

^a UNIVERSITY OF CANTERBURY   (New Zealand)

^b UNIVERSITY OF AUCKLAND   (New Zealand)

Author keywords

Allosteric regulation; Domain interface; Leucine biosynthesis; Multi domain; Mycobacterium tuberculosis; Protein asymmetry

Indexed keywords

2 ISOPROPYLMALATE SYNTHASE; BACTERIAL PROTEIN;

ALLOSTERISM; AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME MECHANISM; ENZYME SUBSTRATE; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PURIFICATION; PROTEIN SYNTHESIS; SUBSTITUTION REACTION; WILD TYPE;

MYCOBACTERIUM TUBERCULOSIS;

EID: 84877664558     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.02.092     Document Type: Article

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