The enzymology of cystathionine biosynthesis: strategies for the control of substrate and reaction specificity

被引：59

作者：

Aitken, SM ^{[1
]}

Kirsch, JF

机构：

[1] Carleton Univ, Dept Biol, Ottawa, ON K1S 5B6, Canada

[2] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2005年 / 433卷 / 01期

关键词：

pyridoxal 5 '-phosphate; reaction specificity; cystathionine; sulfur amino acid; cysteine; homocysteine; methionine;

D O I：

10.1016/j.abb.2004.08.024

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 ability of enzymes to catalyze specific reactions, while excluding others, is central to cellular metabolism. Control of reaction specificity is of particular importance for enzymes that employ catalytically versatile cofactors, of which pyridoxal 5'-phosphate is a prime example. Cystathionine gamma-synthase and cystathionine P-synthase are the first enzymes in the transsulfuration and reverse transsulfuration pathways, respectively. Each of them occupies branch-point positions in amino acid metabolism and as such are subject to transcriptional and post-translational regulation. Both enzymes catalyze the pyridoxal 5'-phosphate-dependent formation of L-cystathionine; however, their substrate and reaction specificities are distinct. The mechanisms whereby these enzymes control the chemistry of the cofactor are the subject of this review. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：166 / 175

页数：10

共 90 条

[51] The human cDNA for a homologue of the plant enzyme 1-aminocyclopropane-1-carboxylate synthase encodes a protein lacking that activity [J].