Ribonuclease 4, an evolutionarily highly conserved member of the superfamily |
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Authors: | J Hofsteenge A Vicentini O Zelenko |
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Institution: | (1) Friedrich Miescher Institute, P.O. Box 2543, CH-4002 Basel (Switzerland), Fax +41 61 697 39 76, CH |
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Abstract: | The structural and enzymatic properties of RNase 4 are reviewed. This RNase shows a much higher interspecies similarity (approximately
90%) than the other members of the RNase A superfamily. The enzyme is ubiquitous, with the highest amounts present in liver
and lung. Its unique uridine specificity results from alterations in and around the pyrimidine-binding site. In particular,
the shortened C-terminus and the side chains of Phe-42, Asp-80 and Arg-101 appear to be involved. RNase 4 binds tightly to
the intracellular RNase inhibitor, with a K
d of 4 × 10−15 M. |
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Keywords: | , RNase substrate specificity, RNase evolution, RNase inhibitor, |
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