Prediction of the structure and function of AstA and AstB, the first two enzymes of the arginine succinyltransferase pathway of arginine catabolism

FEBS Letters

Shirai, Hiroki¹  Mizuguchi, Kenji¹ 

[1]Department of Biochemistry, University of Cambridge, Old Addenbrooks Site, 80 Tennis Court Road, Cambridge CB2 1GA, UK

关键词: Fold recognition;    FUGUE;    Enzyme function;    Protein structure;    Metabolic pathway;   

DOI  :  10.1016/S0014-5793(03)01314-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Arginine succinyltransferase and succinylarginine dihydrolase catalyze the first two steps of arginine catabolism by the arginine succinyltransferase pathway. This route is the only major arginine catabolic pathway in Escherichia coli including its pathogenic strains O157 and CFT073. We have used fold recognition tools and identified novel homologies between each of these two enzymes and proteins of known three-dimensional structure: arginine succinyltransferase belongs to the acyl-CoA N-acyltransferase superfamily and succinylarginine dihydrolase belongs to the amidinotransferase superfamily. These findings shed light on the structures, catalytic mechanisms and evolution of diverse enzymes involved in arginine catabolism.

【 授权许可】

Unknown