Analysis of membrane stereochemistry with homology modeling of sn-glycerol-1-phosphate dehydrogenase

被引:28
作者
Daiyasu, H
Hiroike, T
Koga, Y
Toh, H
机构
[1] Biomol Engn Res Inst, Dept Computat Biol, Suita, Osaka 5650874, Japan
[2] Univ Occupat & Environm Hlth, Dept Chem, Sch Med, Yahatanishi Ku, Kitakyushu, Fukuoka 8078555, Japan
来源
PROTEIN ENGINEERING | 2002年 / 15卷 / 12期
关键词
Archaea; chirality; glycerol phosphate dehydrogenase; membrane;
D O I
10.1093/protein/15.12.987
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
Different enantiomeric isomers, sn-glycerol-1-phosphate and sn-glycerol-3-phosphate, are used as the glycerophosphate backbones of phospholipids in the cellular membranes of Archaea and the remaining two kingdoms, respectively. In Archaea, sn-glycerol-1-phosphate dehydrogenase is involved in the generation of sn-glycerol-1-phosphate, while sn-glycerol-3-phosphate dehydrogenase synthesizes the enantiomer in Eukarya and Bacteria. The coordinates of sn-glycerol-3-phosphate dehydrogenase are available, although neither the tertiary structure nor the reaction mechanism of sn-glycerol-1-phosphate dehydrogenase is known. Database searching revealed that the archaeal enzyme shows sequence similarity to glycerol dehydrogenase, dehydroquinate synthase and alcohol dehydrogenase IV. The glycerol dehydrogenase, with coordinates that are available today, is closely related to the archaeal enzyme. Using the structure of glycerol dehydrogenase as the template, we built a model structure of the Methanothermobacter thermautotrophicus sn-glycerol-1-phosphate dehydrogenase, which could explain the chirality of the product. Based on the model structure, we determined the following: (1) the enzyme requires a Zn2+ ion for its activity; (2) the enzyme selectively uses the pro-R hydrogen of the NAD(P)H; (3) the putative active site and the reaction mechanism were predicted; and (4) the archaeal enzyme does not share its evolutionary origin with sn-glycerol-3-phosphate dehydrogenase.
引用
收藏
页码:987 / 995
页数:9
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