Role of tryptophan hydroxylase Phe313 in determining substrate specificity
Role of tryptophan hydroxylase Phe313 in determining substrate specificity
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DOI：
10.1006/bbrc.2002.6719
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发表时间：
2002-04-05
影响因子：
3.1
通讯作者：
Fitzpatrick, PF
中科院分区：
文献类型：
--
作者：
Daubner, SC;Moran, GR;Fitzpatrick, PF
活性中心残基苯丙氨酸313在所有已知色氨酸羟基酶的序列中都是保守的。色氨酸羟化酶F313W突变蛋白不再显示出对色氨酸的偏好而不是苯丙氨酸作为底物，这与该残基在底物特异性中的作用是一致的。色氨酸残基在酪氨酸羟化酶中占据同源位置。酪氨酸羟化酶W372F突变酶对色氨酸的偏好没有超过酪氨酸或苯丙氨酸，因此该残基不能被认为是该酶家族底物专一性的主导因素。(C)2002年埃尔塞维尔科学公司(美国)。
The active site residue phenylalanine 313 is conserved in the sequences of all known tryptophan hydroxylases. The tryptophan hydroxylase F313W mutant protein no longer shows a preference for tryptophan over phenylalanine as a substrate, consistent with a role of this residue in substrate specificity. A tryptophan residue occupies the homologous position in tyrosine hydroxylase. The tyrosine hydroxylase W372F mutant enzyme does not show an increased preference for tryptophan over tyrosine or phenylalanine, so that this residue cannot be considered the dominant factor in substrate specificity in this family of enzymes. (C) 2002 Elsevier Science (USA).