Southan C, DeWolf W E, Kruse L I
Department of Medicinal Chemistry, Smith Kline & French Research Limited, Welwyn, U.K.
Biochim Biophys Acta. 1990 Feb 9;1037(2):256-8. doi: 10.1016/0167-4838(90)90176-g.
p-Cresol is a mechanism-based inhibitor of bovine dopamine beta-hydroxylase (3,4-dihydroxyphenethylamine, ascorbate: oxygen oxidoreductase (beta-hydroxylating), EC 1.14.17.1) (DBH) which covalently modifies a tyrosine at position 216 during inactivation (DeWolf, W.E., Jr., Carr, S.A., Varrichio, A., Goodhart, P.J., Mentzer, M.A., Roberts, G.D., Southan, C., Dolle, R.E. and Kruse, L.I. (1988) Biochemistry 27, 9093-9101). Here we report the recovery and characterization of additional minor peptides that are produced during the inactivation of DBH with p-[3H]cresol. Sequence and structural analysis of these peptides indicates tyrosine 357 as a second, minor site of modification.
对甲酚是一种基于机制的牛多巴胺β-羟化酶（3,4-二羟基苯乙胺，抗坏血酸：氧氧化还原酶（β-羟化），EC 1.14.17.1）（DBH）抑制剂，在失活过程中它会共价修饰216位的酪氨酸（DeWolf，W.E.，Jr.，Carr，S.A.，Varrichio，A.，Goodhart，P.J.，Mentzer，M.A.，Roberts，G.D.，Southan，C.，Dolle，R.E.和Kruse，L.I.（1988年）《生物化学》27卷，9093 - 9101页）。在此我们报告在用对-[3H]甲酚使DBH失活过程中产生的其他次要肽段的回收及特性鉴定。对这些肽段的序列和结构分析表明酪氨酸357是第二个次要修饰位点。
