Substrate specificity of methylthioadenosine phosphorylase from human liver.
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.
Fabianowska-Majewska
K
K
Department of General Chemistry, Medical University of Lódź, Poland.
Duley
J
J
Fairbanks
L
L
Simmonds
A
A
Wasiak
T
T
D006801:Humans; D008099:Liver / Q000201:enzymology*; D011683:Purine-Nucleoside Phosphorylase / Q000378:metabolism*; D013379:Substrate Specificity
D011683:Purine-Nucleoside Phosphorylase; C021784:5'-methylthioadenosine phosphorylase