大鼠肝脏中的核苷单磷酸酰胺水解酶：纯化与特性鉴定

Nucleoside monophosphoramidate hydrolase from rat liver: purification and characterization.

Kuba M, Okizaki T, Ohmori H, Kumon A

Department of Biochemistry, Saga Medical School, Japan.

Int J Biochem. 1994 Feb;26(2):235-45. doi: 10.1016/0020-711x(94)90151-1.

Abstract

Adenosine 5'-phosphoramidate hydrolase of 29 kDa was isolated from rat liver cytosol. 2. It consisted of two subunits of 14 kDa. 3. It hydrolyzed nucleoside 5'-monophosphoramidates into nucleoside 5'-monophosphates and ammonia, while it did not hydrolyze adenylyl phosphoramidate, adenylyl imidodiphosphate and N-phosphorylated compounds like phosphocreatine, N omega-phosphoarginine, 6-phospholysine and 3-phosphohistidine. 4. Divalent cations and cyclic AMP had no effect on the hydrolytic activity.

摘要

从大鼠肝细胞溶胶中分离出了29 kDa的腺苷5'-磷酸酰胺水解酶。2. 它由两个14 kDa的亚基组成。3. 它将核苷5'-单磷酸酰胺水解为核苷5'-单磷酸和氨，而不水解腺苷酰磷酸酰胺、腺苷酰亚氨基二磷酸以及诸如磷酸肌酸、Nω-磷酸精氨酸、6-磷酸赖氨酸和3-磷酸组氨酸等N-磷酸化化合物。4. 二价阳离子和环磷酸腺苷对水解活性没有影响。