作者: Daniel B. Fisher , Seymour Kaufman
DOI: 10.1016/S0021-9258(19)43778-2
关键词: Tyrosine hydroxylase 、 Enzyme 、 Chymotrypsin 、 Hydroxylation 、 Saturation vapor curve 、 Phenylalanine 、 Tetrahydrobiopterin 、 Chemistry 、 Stereochemistry 、 Phenylalanine hydroxylase 、 Biochemistry 、 Cell biology 、 Molecular biology
摘要: In the presence of natural cofactor, tetrahydrobiopterin, rat liver phenylalanine hydroxylase has a sigmoidal saturation curve (Hill coefficient 2.0) for concentration versus initial velocity. Lysolecithin or α-chymotrypsin increases maximum velocity 20-fold, decreases Km by 50%, and converts phenylalanine-saturation from to hyperbolic form. stimulator increase activity in synergistic fashion. also stimulates hydroxylation tryptophan (to 5-hydroxytryptophan) meta-tyrosine 3,4-dihydroxyphenylalanine) highly purified hydroxylase. para-tyrosine-dependent TPNH oxidation without para-tyrosine. exposes sulfhydryl group therefore appears alter conformation enzyme. Chymotrypsin, contrast, partially hydrolyzes hydroxylase, reducing its size dimer with molecular weight 100,000 (composed two 50,000 subunits) 67,000 35,000 subunits).