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

doi:10.1271/bbb.61.1913

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Article

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...

Topics

Dinucleoside Phosphates
Endoribonucleases
Hydrolysis
Kinetics
Mutagenesis, Site-Directed
Mutation
Nucleotides
RNA
Rhizopus
Substrate Specificity

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