X-ray crystallographic and NMR studies of pantothenate synthetase provide insights into the mechanism of homotropic inhibition by pantoate

FEBS Journal

Volumn 277, Issue 3, 2010, Pages 697-712

  Chakrabarti, Kalyan Sundar ^a   Thakur, Krishan Gopal ^a   Gopal, B ^a   Sarma, Siddhartha P ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

Competitive inhibition; NMR; Pantothenate biosynthesis; Substrate binding; X ray crystallography

Indexed keywords

ADENOSINE TRIPHOSPHATE; ENZYME INHIBITOR; NITROGEN 15; PANTOATE; PANTOTHENATE SYNTHETASE; SYNTHETASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CHEMICAL BINDING; ENZYME ANALYSIS; ENZYME BINDING; ENZYME INHIBITION; ESCHERICHIA COLI; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; X RAY CRYSTALLOGRAPHY;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; BINDING SITES; BINDING, COMPETITIVE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HYDROXYBUTYRATES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE SYNTHASES; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

ESCHERICHIA COLI;

EID: 75149184076     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.07515.x     Document Type: Article

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