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

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

International journal of biological macromolecules - 1 Oct 2011

Liu Na, Wang Jin-Song, Wang Wei-Dong, Pan Ji-Cheng

Abstract excerpt

The purpose of this study is to clarify that the amino acid residues (Asp62 and Arg193) are responsible for the activity and stability of arginine kinase (AK). The amino acid residues Asp62 (D62) and Arg193 (R193) are strictly conserved in monomeric AKs and form an ion pair in the transition state analogue complex. In this research, we replaced D62 with glutamate (E) or glycine (G) and R193 with lysine (K) or...

Read the complete abstract on PubMed

Topics

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

Share to Enzyme Stability
Share to Hydrogen Bonding

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

Share to Models, Molecular

Share to Mutagenesis, Site-Directed

Share to Penaeidae

Share to Protein Binding

Share to Protein Conformation

Share to Protein Unfolding

Source

Identifiers

PMID: 21645540
DOI: 10.1016/j.ijbiomac.2011.05.022

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

The interaction between residues 62 and 193 play a key role in activity and structural stability of arginine kinase.PMID 21645540Read ↗

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

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

T273 plays an important role in the activity and structural stability 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 ↗

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

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

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

Insights on the participation of Glu256 and Asp204 in the oligomeric structure and cooperative effects of human arginase type I.Semantic proximity Read ↗

The role of Arg-96 in Danio rerio creatine kinase in substrate recognition and active center configuration.Semantic proximity Read ↗

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