Shirai Hiroki, Mizuguchi Kenji
Department of Biochemistry, University of Cambridge, Old Addenbrooks Site, 80 Tennis Court Road, Cambridge, CB2 1GA, UK.
FEBS Lett. 2003 Dec 18;555(3):505-10. doi: 10.1016/s0014-5793(03)01314-0.
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.
精氨酸琥珀酰转移酶和琥珀酰精氨酸二水解酶催化精氨酸通过精氨酸琥珀酰转移酶途径进行分解代谢的前两个步骤。这条途径是大肠杆菌（包括其致病菌株O157和CFT073）中唯一主要的精氨酸分解代谢途径。我们使用了折叠识别工具，并确定了这两种酶与已知三维结构的蛋白质之间的新同源性：精氨酸琥珀酰转移酶属于酰基辅酶A N-酰基转移酶超家族，琥珀酰精氨酸二水解酶属于脒基转移酶超家族。这些发现揭示了参与精氨酸分解代谢的多种酶的结构、催化机制和进化。
