Site-directed mutagenesis and deletion of the carboxyl terminus of Escherichia coli ribonucleotide reductase protein R2. Effects on catalytic activity and subunit interaction.

doi:10.1021/bi00135a009

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Article

Site-directed mutagenesis and deletion of the carboxyl terminus of Escherichia coli ribonucleotide reductase protein R2. Effects on catalytic activity and subunit interaction.

Biochemistry - 26 May 1992

Climent I, Sjöberg B M, Huang C Y

Abstract excerpt

Ribonucleotide reductase from Escherichia coli consists of two dissociable, nonidentical homodimeric proteins called R1 and R2. The role of the C-terminal region of R2 in forming the R1R2 active complex has been studied. A heterodimeric R2 form with a full-length polypeptide chain and a truncated one missing the last 30 carboxyl-terminal residues was engineered by site-directed mutagenesis. Kinetic analysis of...

Topics

Bacterial Proteins
Base Sequence
Catalysis
Centrifugation, Density Gradient
Chromosome Deletion
Escherichia coli
Genetic Complementation Test
Kinetics
Molecular Sequence Data
Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Peptide Fragments

Protein Conformation

Recombinant Proteins

Ribonucleotide Reductases

Structure-Activity Relationship

Substrate Specificity

Source

Open in PubMed

Identifiers

PMID: 1591241
DOI: 10.1021/bi00135a009

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1591241-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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