Nucleoside diphosphate kinase from Escherichia coli.

doi:10.1128/jb.177.9.2524-2529.1995

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Nucleoside diphosphate kinase from Escherichia coli.

Journal of bacteriology - 1 May 1995

Almaula N, Lu Q, Delgado J, Belkin S, Inouye M

Abstract excerpt

Nucleoside diphosphate (NDP) kinase from Escherichia coli was purified to homogeneity and was crystallized. Gel filtration analysis of the purified enzyme indicated that it forms a tetramer. The enzyme was phosphorylated with [gamma-32P]ATP, and the pH stability profile of the phosphoenzyme indicated that two different amino acid residues were phosphorylated. Both a histidine residue and serine residues,...

Topics

Adenosine Triphosphate
Amino Acid Sequence
Cloning, Molecular
Crystallization
Enzyme Stability
Escherichia coli
Histidine
Hydrogen-Ion Concentration
Molecular Sequence Data
Mutation
Nucleoside-Diphosphate Kinase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Peptide Fragments

Phosphoproteins

Phosphorylation

Phosphoserine

Protein Conformation

Recombinant Proteins

Sequence Analysis

Source

Open in PubMed Open full text

Identifiers

PMID: 7730286
DOI: 10.1128/jb.177.9.2524-2529.1995
PMCID: PMC176913

Genes

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7730286-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Nucleoside diphosphate kinase from Escherichia coli.PMID 7730286Read ↗

Intermolecular phosphotransfer is crucial for efficient catalytic activity of nucleoside diphosphate kinase.Semantic proximity Read ↗

The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains.Semantic proximity Read ↗

The gene for nucleoside diphosphate kinase functions as a mutator gene in Escherichia coli.Semantic proximity Read ↗

Structural basis for nucleotide binding and reaction catalysis in mevalonate diphosphate decarboxylase.Semantic proximity Read ↗

Isolation and characterization of mutated mitochondrial GTP:AMP phosphotransferase.Semantic proximity Read ↗

Engineering of halophilic enzymes: two acidic amino acid residues at the carboxy-terminal region confer halophilic characteristics to Halomonas and Pseudomonas nucleoside diphosphate kinases.Semantic proximity Read ↗

Enhancement of nucleoside phosphorylation activity in an acid phosphatase.Semantic proximity Read ↗

Cys139Ser mutation in dimeric nucleoside diphosphate kinase generates catalytically competent monomer.Semantic proximity Read ↗

Structurally and catalytically important residues in the phosphate binding loop of adenylate kinase of Escherichia coli.Semantic proximity Read ↗

Two glutamate residues, Glu 208 alpha and Glu 197 beta, are crucial for phosphorylation and dephosphorylation of the active-site histidine residue in succinyl-CoA synthetase.Semantic proximity Read ↗

[Protein engineering of uridine phosphorylase from Escherichia coli K-12. II. Comparative study of hybrid and mutant forms of uridine phosphorylases].Semantic proximity Read ↗

Catalytic site of F1-ATPase of Escherichia coli. Lys-155 and Lys-201 of the beta subunit are located near the gamma-phosphate group of ATP in the presence of Mg2+.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.