ATP binding to human serine racemase is cooperative and modulated by glycine.
about
Serine racemase: a key player in apoptosis and necrosisHarnessing allostery: a novel approach to drug discovery.Human serine racemase structure/activity relationship studies provide mechanistic insight and point to position 84 as a hot spot for β-elimination function.Kinetic characterization of the human O-phosphoethanolamine phospho-lyase reveals unconventional features of this specialized pyridoxal phosphate-dependent lyase.Cyclopropane derivatives as potential human serine racemase inhibitors: unveiling novel insights into a difficult target.Regulation of human serine racemase activity and dynamics by halides, ATP and malonateCrystal structure of maize serine racemase with pyridoxal 5'-phosphate.Glutamine 89 is a key residue in the allosteric modulation of human serine racemase activity by ATP.
P2860
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P2860
ATP binding to human serine racemase is cooperative and modulated by glycine.
description
2013 nî lūn-bûn
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2013年の論文
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2013年学术文章
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2013年学术文章
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name
ATP binding to human serine racemase is cooperative and modulated by glycine.
@en
ATP binding to human serine racemase is cooperative and modulated by glycine.
@nl
type
label
ATP binding to human serine racemase is cooperative and modulated by glycine.
@en
ATP binding to human serine racemase is cooperative and modulated by glycine.
@nl
prefLabel
ATP binding to human serine racemase is cooperative and modulated by glycine.
@en
ATP binding to human serine racemase is cooperative and modulated by glycine.
@nl
P2093
P2860
P50
P356
P1433
P1476
ATP binding to human serine racemase is cooperative and modulated by glycine.
@en
P2093
Barbara Campanini
Marialaura Marchetti
Nicole Mai
P2860
P304
P356
10.1111/FEBS.12510
P407
P577
2013-09-25T00:00:00Z