Hybrid tetramers reveal elements of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase.
about
The effect of hinge mutations on effector binding and domain rotation in Escherichia coli D-3-phosphoglycerate dehydrogenaseD-3-Phosphoglycerate dehydrogenase from Mycobacterium tuberculosis is a link between the Escherichia coli and mammalian enzymesDiscovery of novel allosteric effectors based on the predicted allosteric sites for Escherichia coli D-3-phosphoglycerate dehydrogenaseTransient kinetic analysis of the interaction of L-serine with Escherichia coli D-3-phosphoglycerate dehydrogenase reveals the mechanism of V-type regulation and the order of effector bindingContrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases.Quantitative relationships of site to site interaction in Escherichia coli D-3-phosphoglycerate dehydrogenase revealed by asymmetric hybrid tetramers.Transient kinetic analysis of L-serine interaction with Escherichia coli D-3-phosphoglycerate dehydrogenase containing amino acid mutations in the hinge regions.Identification of amino acid residues contributing to the mechanism of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase.
P2860
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P2860
Hybrid tetramers reveal elements of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase.
description
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name
Hybrid tetramers reveal elemen ...... hosphoglycerate dehydrogenase.
@en
Hybrid tetramers reveal elemen ...... hosphoglycerate dehydrogenase.
@nl
type
label
Hybrid tetramers reveal elemen ...... hosphoglycerate dehydrogenase.
@en
Hybrid tetramers reveal elemen ...... hosphoglycerate dehydrogenase.
@nl
prefLabel
Hybrid tetramers reveal elemen ...... hosphoglycerate dehydrogenase.
@en
Hybrid tetramers reveal elemen ...... hosphoglycerate dehydrogenase.
@nl
P2093
P2860
P356
P1476
Hybrid tetramers reveal elemen ...... hosphoglycerate dehydrogenase.
@en
P2093
Gregory A Grant
Xiao Lan Xu
P2860
P304
18170-18176
P356
10.1074/JBC.M213050200
P407
P577
2003-03-18T00:00:00Z