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Substrate specificity of methylthioadenosine phosphorylase from human liver

100%

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

Acta Biochimica Polonica

1994

tom 41

nr 4

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-chloro- adenosine > 2-chloro-5'-0-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.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Duley J.

1 Fabianowska-Majewska K.

1 Fairbanks L.

1 Simmonds A.

1 Wasiak T.

1 1994

Wyniki wyszukiwania

Substrate specificity of methylthioadenosine phosphorylase from human liver