Metal-characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1.
作者信息
Wakayama M, Miura Y, Oshima K, Sakai K, Moriguchi M
机构信息
Department of Applied Chemistry, Faculty of Engineering, Oita University, Japan.
出版信息
Biosci Biotechnol Biochem. 1995 Aug;59(8):1489-92. doi: 10.1271/bbb.59.1489.
PMID:7549100
Abstract
N-Acyl-D-glutamate amidohydrolase (D-AGase) from Pseudomonas sp. 5f-1 was a zinc-metalloenzyme which contained 2.06-2.61 g.atom of Zn per mole of enzyme. The zinc atom was required for the catalytic activity and stability of the enzyme. The N-terminal amino acid sequence of Pseudomonas sp. 5f-1 D-AGase showed 32% identity to that of Alcaligenes xylosoxydans subsp. xylosoxydans A-6.
摘要
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