A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase

Proceedings of the National Academy of Sciences of the United States of America

Volumn 104, Issue 21, 2007, Pages 8815-8820

  Velyvis, Algirdas ^a   Yang, Ying R ^b   Schachman, Howard K ^b   Kay, Lewis E ^a  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Allostery; Ligand binding; Methyl transverse relaxation optimized spectroscopy; Monod Wyman Changeux (MWC) model; NMR spectroscopy

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE; LIGAND; NUCLEOTIDE DERIVATIVE; NUCLEOTIDE;

ALLOSTERISM; ARTICLE; ENZYME ACTIVE SITE; ENZYME BINDING; LIGAND BINDING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; BINDING SITE; CHEMISTRY; ENZYME SPECIFICITY; METABOLISM; METHYLATION; NUCLEAR MAGNETIC RESONANCE; PROTEIN BINDING; TITRIMETRY;

ALLOSTERIC REGULATION; ASPARTATE CARBAMOYLTRANSFERASE; BINDING SITES; LIGANDS; METHYLATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; NUCLEOTIDES; PROTEIN BINDING; SUBSTRATE SPECIFICITY; TITRIMETRY;

EID: 34547399613     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0703347104     Document Type: Article

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