Open AccessSubstrate specificity of methylthioadenosine phosphorylase from human liver.
Author(s) -
Krystyna FabianowskaMajewska,
John A. Duley,
Lynette D. Fairbanks,
Anne Simmonds,
T. Wasiak
Publication year - 1994
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.1994_4683
Subject(s) - phosphorolysis , deoxyadenosine , purine nucleoside phosphorylase , chemistry , thymidine phosphorylase , biochemistry , adenosine , enzyme , nucleoside , purine
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.