title: Substrate specificity of methylthioadenosine phosphorylase from human liver.
abstract: Methylthioadenosine (MTA) phosphorylase purified 615-fold from human liver cleaved phosphorolytically nucleoside analogues at the decreasing specific activity: 5'-deoxyadenosine > 5'-iodo-5'-deoxyadenosine > MTA > adenosine > 2-chloroadenosine > 2-chloro-5'-O-methyl-2'-deoxyadenosine > 2-chloro-2'-deoxyadenosine > > 2'-deoxyadenosine. Adenosine and analogues of 5'-deoxyadenosine were strong competitive inhibitors of MTA phosphorolysis catalysed by the human liver enzyme.
authors.affiliation: Department of General Chemistry, Medical University of Lódź, Poland.
authors.forename: K
authors.initials: K
authors.lastname: Fabianowska-Majewska
authors.forename: J
authors.initials: J
authors.lastname: Duley
authors.forename: L
authors.initials: L
authors.lastname: Fairbanks
authors.forename: A
authors.initials: A
authors.lastname: Simmonds
authors.forename: T
authors.initials: T
authors.lastname: Wasiak
mesh_terms: D006801:Humans; D008099:Liver / Q000201:enzymology*; D011683:Purine-Nucleoside Phosphorylase / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D011683:Purine-Nucleoside Phosphorylase; C021784:5'-methylthioadenosine phosphorylase