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Title: Substrate specificity of methylthioadenosine phosphorylase from human liver. Author: Fabianowska-Majewska K, Duley J, Fairbanks L, Simmonds A, Wasiak T. Journal: Acta Biochim Pol; 1994; 41(4):391-5. PubMed ID: 7732755. 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.[Abstract] [Full Text] [Related] [New Search]