Examination of a reaction intermediate in the active site of riboflavin synthase

被引：3

作者：

Zheng, YJ

Jordan, DB

Liao, DI

机构：

[1] DuPont Co Inc, Agr Prod, Stine Haskell Res Ctr, Newark, DE 19714 USA

[2] DuPont Co Inc, Cent Res & Dev, Expt Stn, Wilmington, DE 19880 USA

来源：

BIOORGANIC CHEMISTRY | 2003年 / 31卷 / 04期

关键词：

riboflavin synthase; riboflavin biosynthesis; catalytic mechanism; enzyme mechanism; stereochemistry; modeling; X-ray crystallography; structure-based design;

D O I：

10.1016/S0045-2068(03)00029-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The riboflavin synthase catalyzed reaction proceeds through a pentacyclic intermediate of undetermined stereochemistry. Calculations at the B3LYP/6-31G(d) level of theory indicate that the trans pentacyclic structure is favored over the cis by 3.3kcal/mol. A model of the the trans, but not the cis, pentacycle in the enzyme active site shows good fitness and the availability of highly conserved protein residues for catalytic interactions. The model of the trans intermediate complements the model of the two substrates in the active site and allows for a hypothetical mechanism of the roles of specific protein residues in catalysis to be proposed. (C) 2003 Elsevier Science (USA). All rights reserved.

引用

页码：278 / 287

页数：10

共 21 条

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