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Enzymatic properties of double mutant enzymes at Asp51 and Trp49 and Asp51 and Tyr57 of RNase Rh from Rhizopus niveus.

Bioscience, biotechnology, and biochemistry - 1 Nov 1997

Ohgi K, Takeuchi M, Iwama M, Irie M

Abstract excerpt

Mutation of Asp51 of a base-nonspecific RNase, RNase Rh, to Ser, Thr, or Gln makes the enzyme more preferential for the dinucleoside phosphate (XpY) having G and C at the 5'-side (X). On the other hand the mutation of one of the B1 site components, Tyr57 to Trp, and Trp49 to Phe makes the enzyme more preferential for purine bases and pyrimidine bases, respectively. In this study, to obtain more specific RNases...

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PMID: 9404071
DOI: 10.1271/bbb.61.1913

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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