Interaction of human 3-phosphoglycerate kinase with its two substrates: Is substrate antagonism a kinetic advantage?

Journal of Molecular Biology

Volumn 409, Issue 5, 2011, Pages 742-757

  Lallemand, Perrine ^a   Chaloin, Laurent ^a   Roy, Béatrice ^b   Barman, Tom ^a   Bowler, Matthew W ^c   Lionne, Corinne ^a  

^a University of Montpellier I and II   (France)

^b UNIVERSITÉ DE MONTPELLIER   (France)

^c EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

Author keywords

crystallographic structure; rapid quench flow; stopped flow; transient kinetics; transition state analogue

Indexed keywords

3 PHOSPHOGLYCERIC ACID; ADENOSINE DIPHOSPHATE; GLYCERIC ACID; PHOSPHOGLYCERATE KINASE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DISSOCIATION CONSTANT; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN METABOLISM; PROTEIN STABILITY; STEADY STATE;

EID: 79958051803     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.04.048     Document Type: Article

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