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Article

Role of Lys108 in the enzymatic activity of RNase Rh from Rhizopus niveus.

Journal of biochemistry - 1 Jan 1995

Ohgi K, Iwama M, Tada K, Takizawa R, Irie M

Abstract excerpt

In order to elucidate on the mechanism of action of RNase Rh from Rhizopus niveus, we investigated the role of Lys108, which is conserved among the RNase T2 family RNases except for two cases. The RNase activities of Lys108 mutant RNases, RNase RNAP K108R and K108L, are about 33.5 and 3.1% of that of the wild type enzyme, respectively. The relative rates of cleavage of dinucleoside phosphates by these two mutant...

Topics

Amino Acid Sequence
Base Sequence
Binding Sites
Circular Dichroism
Crystallography, X-Ray
Endoribonucleases
Genes, Fungal
Lysine
Molecular Sequence Data
Molecular Structure
Multigene Family

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Nucleotides

Rhizopus

Structure-Activity Relationship

Source

Identifiers

PMID: 7775395
DOI: 10.1093/oxfordjournals.jbchem.a124716

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7775395-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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