Substrate specificity of methylthioadenosine phosphorylase from human liver

Autor: K, Fabianowska-Majewska, J, Duley, L, Fairbanks, A, Simmonds, T, Wasiak
Rok vydání: 1994
Předmět:
Zdroj: Acta biochimica Polonica. 41(4)
ISSN: 0001-527X
Popis: Methylthioadenosine (MTA) phosphorylase purified 615-fold from human liver cleaved phosphorolytically nucleoside analogues at the decreasing specific activity: 5'-deoxyadenosine5'-iodo-5'-deoxyadenosineMTAadenosine2-chloroadenosine2-chloro-5'-O-methyl-2'-deoxyadenosine2-chloro-2'-deoxyadenosine2'-deoxyadenosine. Adenosine and analogues of 5'-deoxyadenosine were strong competitive inhibitors of MTA phosphorolysis catalysed by the human liver enzyme.
Databáze: OpenAIRE