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EC Number	Crystallization (Commentary)
2.5.1.140	in presence of O-phospho-L-serine. Formation of the pyridoxal phosphate-alpha-aminoacrylate intermediate induces closure of the active site pocket by narrowing the channel leading to the active site and forming a second substrate binding pocket that likely binds L-glutamate. Active site residues Arg132, Tyr152, Ser185 are essential for O-phospho-L-serine recognition and turnover. Mutations Y152F/S185G induce a closed form of the enzyme in the absence of the alpha-aminoacrylate intermediate

EC Number

Crystallization (Commentary)

2.5.1.140

in presence of O-phospho-L-serine. Formation of the pyridoxal phosphate-alpha-aminoacrylate intermediate induces closure of the active site pocket by narrowing the channel leading to the active site and forming a second substrate binding pocket that likely binds L-glutamate. Active site residues Arg132, Tyr152, Ser185 are essential for O-phospho-L-serine recognition and turnover. Mutations Y152F/S185G induce a closed form of the enzyme in the absence of the alpha-aminoacrylate intermediate

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Release 2023.1 (January 2023)