Revealing Substrate Promiscuity of 1-Deoxy-D-xylulose 5-Phosphate Synthase

被引：38

作者：

Brammer, Leighanne A. ^{[1
]}

Meyers, Caren Freel ^{[1
]}

机构：

[1] Johns Hopkins Univ, Sch Med, Dept Pharmacol & Mol Sci, Baltimore, MD 21205 USA

来源：

ORGANIC LETTERS | 2009年 / 11卷 / 20期

关键词：

ESCHERICHIA-COLI; ISOPENTENYL DIPHOSPHATE; ISOPRENOID BIOSYNTHESIS; RHODOBACTER-CAPSULATUS; ENZYMATIC-SYNTHESIS; CLONING; PATHWAY; GENE; INHIBITORS; ENZYMES;

D O I：

10.1021/ol901961q

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

A study of DXP synthase has revealed flexibility in the acceptor substrate binding pocket for nonpolar substrates and has uncovered new details of the catalytic mechanism to show that pyruvate can act as both donor and acceptor substrate.

引用

页码：4748 / 4751

页数：4

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