Kinetic and X-Ray Structural Evidence for Negative Cooperativity in Substrate Binding to Nicotinate Mononucleotide Adenylyltransferase (NMAT) from Bacillus anthracis

Journal of Molecular Biology

Volumn 385, Issue 3, 2009, Pages 867-888

  Sershon, Valerie C ^a   Santarsiero, Bernard D ^a   Mesecar, Andrew D ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

allosteric regulation; anthrax; Koshland Nemethy Filmer; NAD(P); pathway

Indexed keywords

ADENOSINE TRIPHOSPHATE; DIMER; MONOMER; NICOTINIC ACID ADENINE DINUCLEOTIDE PHOSPHATE; NICOTINIC ACID MONONUCLEOTIDE ADENYLYLTRANSFERASE; NUCLEOTIDYLTRANSFERASE; PHOSPHODIESTERASE; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS ANTHRACIS; BINDING AFFINITY; CONFORMATIONAL TRANSITION; DRUG TARGETING; ENZYME BINDING; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; STEADY STATE; X RAY CRYSTALLOGRAPHY;

BACILLUS ANTHRACIS; BACTERIA (MICROORGANISMS); PROKARYOTA;

EID: 58149185108     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.10.037     Document Type: Article

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