An unprecedented twist to ODCase catalytic activity
An unprecedented twist to ODCase catalytic activity
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DOI：
10.1021/ja054865u
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发表时间：
2005-11-02
影响因子：
15
通讯作者：
Kotra, LP
中科院分区：
文献类型：
--
作者：
Fujihashi, M;Bello, AM;Kotra, LP
乳清酸核苷-5 '-单磷酸脱羧酶（ODCase）已经进化为催化脱羧反应，最可能是通过乳清酸核苷-5'-单磷酸的C6位置处的碳负离子物质。我们揭示了一种不寻常的生化途径，即ODCase通过C6位置的亲电中心将6-氰基-尿苷-5 '-单磷酸转化为巴比妥酸盐-5'-单磷酸，从而导致抑制。ODCase的这种潜力在设计新型抑制剂方面非常有用。
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.