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

T273 plays an important role in the activity and structural stability of arginine kinase.

International journal of biological macromolecules - 1 Feb 2014

Wu Qing-Yun, Guo Hua-Yan, Geng Hong-Li, Ru Bian-Mei, Cao Jiang, Chen Chong, Zeng Ling-Yu, Wang Xiao-Yun, Li Feng, Xu Kai-Lin

Abstract excerpt

Arginine kinase (AK) is a key enzyme for cellular energy metabolism, catalyzing the reversible phosphoryl transfer from phosphoarginine to ADP in invertebrates. The amino acid residue C271 is involved in keeping AK's activity and constraining the orientation of the substrate arginine. However, the roles of the C271 interaction amino acid residues in AK's substrate synergism, activity and structural stability are...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Energy Metabolism

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

Share to Kinetics

Share to Mutation

Share to Protein Structure, Tertiary

Share to Substrate Specificity

Source

Identifiers

PMID: 24157705
DOI: 10.1016/j.ijbiomac.2013.10.019

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

T273 plays an important role in the activity and structural stability of arginine kinase.PMID 24157705Read ↗

Val65 plays an important role in the substrate synergism, structural stability and activity of arginine kinase.Semantic proximity Read ↗

The D14 and R138 ion pair is involved in dimeric arginine kinase activity, structural stability and folding.Semantic proximity Read ↗

Impact of intra-subunit interactions on the dimeric arginine kinase activity and structural stability.Semantic proximity Read ↗

Evidence that the amino acid residue P272 of arginine kinase is involved in its activity, structure and stability.Semantic proximity Read ↗

The interaction between residues 62 and 193 play a key role in activity and structural stability of arginine kinase.Semantic proximity Read ↗

The roles of C-terminal loop residues of dimeric arginine kinase from sea cucumber Stichopus japonicus in catalysis, specificity and structure.Semantic proximity Read ↗

Mutation of residue arginine 330 of arginine kinase results in the generation of the oxidized form more susceptible.Semantic proximity Read ↗

Mutation of the conserved G66 residue in GS region decreased structural stability and activity of arginine kinase.Semantic proximity Read ↗

Amino acid residues 62 and 193 play the key role in regulating the synergism of substrate binding in oyster arginine kinase.Semantic proximity Read ↗

Evidence that the amino acid residue Ile121 is involved in arginine kinase activity and structural stability.Semantic proximity Read ↗

The active site cysteine of arginine kinase: structural and functional analysis of partially active mutants.Semantic proximity Read ↗

Roles of amino acid residues H66 and D326 in the creatine kinase activity and structural stability.Semantic proximity Read ↗

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