title: Nucleoside monophosphoramidate hydrolase from rat liver: purification and characterization.
abstract: 1. 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.
authors.affiliation: Department of Biochemistry, Saga Medical School, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Kuba
authors.forename: T
authors.initials: T
authors.lastname: Okizaki
authors.forename: H
authors.initials: H
authors.lastname: Ohmori
authors.forename: A
authors.initials: A
authors.lastname: Kumon
mesh_terms: D000818:Animals; D002499:Centrifugation, Density Gradient; D003600:Cytosol / Q000201:enzymology*; D006867:Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D006868:Hydrolysis; D008099:Liver / Q000201:enzymology* / Q000648:ultrastructure; D011506:Proteins / Q000494:pharmacology; D051381:Rats; D017208:Rats, Wistar; D013379:Substrate Specificity; D014461:Ultracentrifugation
chemical_list: D011506:Proteins; D006867:Hydrolases; C087067:adenosine 5'-phosphoramidate hydrolase