Removal of the C-terminal regulatory domain of α-isopropylmalate synthase disrupts functional substrate binding

Biochemistry

Volumn 51, Issue 11, 2012, Pages 2289-2297

  Huisman, Frances H A ^a   Koon, Nayden ^b   Bulloch, Esther M M ^b   Baker, Heather M ^b   Baker, Edward N ^b   Squire, Christopher J ^b   Parker, Emily J ^a  

^a UNIVERSITY OF CANTERBURY   (New Zealand)

^b UNIVERSITY OF AUCKLAND   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

ALDOL REACTIONS; CATALYTIC DOMAINS; CATALYTIC SITES; COMPLEMENTATION; DIVALENT METAL ION; ESCHERICHIA COLI CELLS; FEEDBACK REGULATION; ISOTHERMAL TITRATION CALORIMETRY; MYCOBACTERIUM TUBERCULOSIS; NEISSERIA MENINGITIDIS; PROTEIN DYNAMICS; REGULATORY DOMAIN; SUBSTRATE BINDING; SUBSTRATE-BOUND; SYNTHASES; WILD TYPES; X RAY CRYSTAL STRUCTURES;

AMINO ACIDS; BIOCHEMISTRY; BIOSYNTHESIS; CATALYSIS; CONDENSATION REACTIONS; ENZYMES; ESCHERICHIA COLI; GENE ENCODING; METAL IONS; PROTEINS;

SUBSTRATES;

2 ISOPROPYLMALATE SYNTHASE; DIMER; ENZYME VARIANT;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME PURIFICATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; ISOTHERMAL TITRATION CALORIMETRY; MOLECULAR CLONING; MYCOBACTERIUM TUBERCULOSIS; NEISSERIA MENINGITIDIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ACTIVITY RELATION; WILD TYPE;

2-ISOPROPYLMALATE SYNTHASE; ACETYL COENZYME A; BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; KETO ACIDS; KINETICS; MYCOBACTERIUM TUBERCULOSIS; NEISSERIA MENINGITIDIS; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI; MYCOBACTERIUM TUBERCULOSIS; NEISSERIA MENINGITIDIS;

EID: 84858638497     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201717j     Document Type: Article

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