Substrate specificity of methylthioadenosine phosphorylase from human liver.

K Fabianowska-Majewska; J Duley; L Fairbanks; A Simmonds; T Wasiak

doi:10.18388/abp.1994_4683

Substrate specificity of methylthioadenosine phosphorylase from human liver.

K Fabianowska-Majewska Department of General Chemistry, Medical University of Lódź, Poland.;
J Duley
L Fairbanks
A Simmonds
T Wasiak

DOI: https://doi.org/10.18388/abp.1994_4683

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.

Published

1994-12-31

Issue

Vol. 41 No. 4 (1994)

Section

Articles

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