Allosteric threonine synthase. Reorganization of the pyridoxal phosphate site upon asymmetric activation through S-adenosylmethionine binding to a novel site.
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Crystal Structure of a Homolog of Mammalian Serine Racemase from Schizosaccharomyces pombeBinding leverage as a molecular basis for allosteric regulationStructure-Based Statistical Mechanical Model Accounts for the Causality and Energetics of Allosteric CommunicationConvergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase.Aspartate-Derived Amino Acid Biosynthesis in Arabidopsis thaliana.Controlling reaction specificity in pyridoxal phosphate enzymes.Evolutionary analysis of a novel zinc ribbon in the N-terminal region of threonine synthase.Identification of cystathionine γ-synthase and threonine synthase from Cicer arietinum and Lens culinaris.
P2860
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P2860
Allosteric threonine synthase. Reorganization of the pyridoxal phosphate site upon asymmetric activation through S-adenosylmethionine binding to a novel site.
description
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name
Allosteric threonine synthase. ...... onine binding to a novel site.
@en
Allosteric threonine synthase. ...... onine binding to a novel site.
@nl
type
label
Allosteric threonine synthase. ...... onine binding to a novel site.
@en
Allosteric threonine synthase. ...... onine binding to a novel site.
@nl
prefLabel
Allosteric threonine synthase. ...... onine binding to a novel site.
@en
Allosteric threonine synthase. ...... onine binding to a novel site.
@nl
P2093
P2860
P356
P1476
Allosteric threonine synthase. ...... onine binding to a novel site.
@en
P2093
Corine Mas-Droux
Renaud Dumas
Valérie Biou
P2860
P304
P356
10.1074/JBC.M509798200
P407
P577
2005-11-29T00:00:00Z