鸟氨酸脱羧酶催化活性出现前所未有的转折。
An unprecedented twist to ODCase catalytic activity.
作者信息
Fujihashi Masahiro, Bello Angelica M, Poduch Ewa, Wei Lianhu, Annedi Subhash C, Pai Emil F, Kotra Lakshmi P
机构信息
Molecular Design and Information Technology Center, Leslie Dan Faculty of Pharmacy, Toronto, ON M5S 2S2 Canada.
出版信息
J Am Chem Soc. 2005 Nov 2;127(43):15048-50. doi: 10.1021/ja054865u.
Orotidine-5'-monophosphate decarboxylase (ODCase) has evolved to catalyze a decarboxylation reaction, most probably via a carbanion species at the C6 position of orotidine-5'-monophosphate. We reveal an unusual biochemical pathway of conversion of 6-cyano-uridine-5'-monophosphate by ODCase to barbiturate-5'-monophosphate via perhaps an electrophilic center at the C6 position, leading to inhibition. This potential of ODCase is very useful in the design of novel inhibitors.
乳清苷-5'-单磷酸脱羧酶（ODCase）已经进化到能够催化脱羧反应，最有可能是通过乳清苷-5'-单磷酸C6位的碳负离子中间体来实现。我们揭示了ODCase将6-氰基-尿苷-5'-单磷酸转化为巴比妥酸-5'-单磷酸的一条不同寻常的生化途径，该途径可能通过C6位的亲电中心，从而导致抑制作用。ODCase的这种特性在新型抑制剂的设计中非常有用。
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