Substrate specificity of methylthioadenosine phosphorylase from human liver. | Zendy

Krystyna FabianowskaMajewska | Zendy; J. A. Duley | Zendy; Lynette D. Fairbanks | Zendy; Anne Simmonds | Zendy; T. WASIAK | Zendy

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Substrate specificity of methylthioadenosine phosphorylase from human liver.

Author(s) -

Krystyna FabianowskaMajewska,

J. 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.

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