Site-directed random mutagenesis of AMP-binding residues in adenylate kinase.

doi:10.1093/oxfordjournals.jbchem.a124228

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Article

Site-directed random mutagenesis of AMP-binding residues in adenylate kinase.

Journal of biochemistry - 1 Nov 1993

Okajima T, Tanizawa K, Fukui T

Abstract excerpt

Two highly conservative residues, Val67 and Gln101, in adenylate kinase are located in the hydrophobic region putatively involved in binding of the adenine ring of AMP. We have performed polymerase chain reaction-based random mutagenesis of the two residues using recombinant chicken muscle adenylate kinase cDNA as a template. The synthetic oligonucleotide primers contained A,G,C,T-mixed bases in the codons...

Topics

Adenosine Monophosphate
Adenylate Kinase
Amino Acid Sequence
Animals
Base Sequence
Binding Sites
Chickens
DNA, Complementary
Escherichia coli
Glutamine
Molecular Sequence Data
Muscles

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutagenesis, Site-Directed

Mutation

Phosphorylation

Polymerase Chain Reaction

Protein Biosynthesis

Recombinant Proteins

Source

Open in PubMed

Identifiers

PMID: 8113212
DOI: 10.1093/oxfordjournals.jbchem.a124228

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8113212-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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