Discover Community Create You

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

Article

Cys139Ser mutation in dimeric nucleoside diphosphate kinase generates catalytically competent monomer.

International journal of biological macromolecules - 1 May 2014

Tokunaga Hiroko, Arakawa Tsutomu, Tokunaga Masao

Abstract excerpt

Nucleoside diphosphate kinase from a moderate halophile Halomonas sp. 593 (HaNDK) is dimer, while NDK from different origins has been shown to assemble into hexamer, or tetramer. Similar to HaNDK, halophilic NDK from Chromohalobacter salexigens DSM3043 (CsNDK) formed dimeric structure. Cysteine139 conserved between HaNDK and CsNDK is located in the monomer/monomer interface. Substitution of Cys139 for Ser caused...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Bacterial Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Catalysis

Share to Circular Dichroism

Share to Cysteine

Share to Escherichia coli

Share to Molecular Sequence Data

Share to Nucleoside-Diphosphate Kinase

Source

Identifiers

PMID: 24548748
DOI: 10.1016/j.ijbiomac.2014.02.016

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cys139Ser mutation in dimeric nucleoside diphosphate kinase generates catalytically competent monomer.PMID 24548748Read ↗

Increase of salt dependence of halophilic nucleoside diphosphate kinase caused by a single amino acid substitution.Semantic proximity Read ↗

Reduction of salt-requirement of halophilic nucleoside diphosphate kinase by engineering S-S bond.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 ↗

Structure, Folding and Stability of Nucleoside Diphosphate Kinases.Semantic proximity Read ↗

Effects of mutations at Gly114 on the stability and refolding of Haloarchaeal nucleoside diphosphate kinase in low salt solution.Semantic proximity Read ↗

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

C-terminal hybrid mutant of Bacillus pumilus cyanide dihydratase dramatically enhances thermal stability and pH tolerance by reinforcing oligomerization.Semantic proximity Read ↗

Delineating the role of ionic interactions in structural and functional integrity of B. malayi Guanylate kinase.Semantic proximity Read ↗

Hydrogen/Deuterium Exchange Mass Spectrometry Reveals Mechanistic Details of Activation of Nucleoside Diphosphate Kinases by Oligomerization.Semantic proximity Read ↗

Distance variations between active sites of H(+)-pyrophosphatase determined by fluorescence resonance energy transfer.Semantic proximity Read ↗

The flexibility of the non-conservative region at the C terminus of D-hydantoinase from Pseudomonas putida YZ-26 is extremely limited.Semantic proximity Read ↗

[Investigation of active center of deoxynucleoside monophosphate kinase of bacteriophage T5 by site-directed mutagenesis].Semantic proximity Read ↗

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