Evolution of enzymes and pathways for the biosynthesis of cofactors

被引：48

作者：

Holliday, Gemma L.

Thornton, Janet M.

Marquet, Andree

Smith, Alison G.

Rebeille, Fabrice

Mendel, Ralf

Schubert, Heidi L.

Lawrence, Andrew D.

Warren, Martin J.

机构：

[1] European Bioinformat Inst, Hinxton CB10 1SD, England

[2] Univ Paris 06, CNRS, Dept Chem, UMR 7613, F-75252 Paris, France

[3] Univ Cambridge, Dept Plant Sci, Cambridge CB2 3EA, England

[4] Univ Grenoble 1, INRA, Inst Rech Technol & Sci Vivant, CEA,CNRS,Lab Physiol Cellular Vegetale,UMR 5168, F-38054 Grenoble, France

[5] Tech Univ Carolo Wilhelmina Braunschweig, Dept Plant Biol, D-38106 Braunschweig, Germany

[6] Univ Utah, Dept Biochem, Salt Lake City, UT 84112 USA

[7] Univ Kent, Dept Biosci, Protein Sci Grp, Canterbury CT2 7NJ, Kent, England

来源：

NATURAL PRODUCT REPORTS | 2007年 / 24卷 / 05期

基金：

英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1039/b703107f

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 evolution of metabolic pathways is discussed with reference to the biosynthesis of a number of vitamins and cofactors. Retrograde and patchwork models are highlighted and their relevance to our knowledge of pathway processes and enzymes is examined. Pathway complexity is explained in terms of the acquisition of broad specificity enzymes.

引用

页码：972 / 987

页数：16

共 106 条

[1] Crystal structure of aspartate decarboxylase at 2.2 Å resolution provides evidence for an ester in protein self-processing [J].