Amino acid residue mutations uncouple cooperative effects in Escherichia coli D-3-phosphoglycerate dehydrogenase.
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The effect of hinge mutations on effector binding and domain rotation in Escherichia coli D-3-phosphoglycerate dehydrogenaseStructural Analysis of Substrate and Effector Binding in Mycobacterium tuberculosis d -3-Phosphoglycerate Dehydrogenase † ‡Structural basis for the catalytic mechanism of homoserine 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.Conformational instability of human prion protein upon residue modification: a molecular dynamics simulation study.Cofactor binding to Escherichia coli D-3-phosphoglycerate dehydrogenase induces multiple conformations which alter effector binding.Hybrid tetramers reveal elements of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase.Flexibility at Gly-194 is required for DNA cleavage and relaxation activity of Escherichia coli DNA topoisomerase I.A single nucleotide polymorphism alters the activity of the renal Na+:Cl- cotransporter and reveals a role for transmembrane segment 4 in chloride and thiazide affinity.
P2860
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P2860
Amino acid residue mutations uncouple cooperative effects in Escherichia coli D-3-phosphoglycerate dehydrogenase.
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name
Amino acid residue mutations u ...... hosphoglycerate dehydrogenase.
@en
Amino acid residue mutations u ...... hosphoglycerate dehydrogenase.
@nl
type
label
Amino acid residue mutations u ...... hosphoglycerate dehydrogenase.
@en
Amino acid residue mutations u ...... hosphoglycerate dehydrogenase.
@nl
prefLabel
Amino acid residue mutations u ...... hosphoglycerate dehydrogenase.
@en
Amino acid residue mutations u ...... hosphoglycerate dehydrogenase.
@nl
P2093
P2860
P356
P1476
Amino acid residue mutations u ...... hosphoglycerate dehydrogenase.
@en
P2093
P2860
P304
17844-17850
P356
10.1074/JBC.M009957200
P407
P577
2001-02-20T00:00:00Z