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

Structural and Biochemical Studies on the Reaction Mechanism of Uridine-Cytidine Kinase.

The protein journal - 1 Dec 2015

Tomoike Fumiaki, Nakagawa Noriko, Kuramitsu Seiki, Masui Ryoji

Abstract excerpt

Uridine-cytidine kinase catalyzes phosphorylation of the pyrimidine nucleosides uridine and cytidine and plays an important role in nucleotide metabolism. However, the detailed molecular mechanism of these reactions remains to be elucidated. Here, we determined the structure of the ternary complex of Uridine-cytidine kinase from Thermus thermophilus HB8 with both cytidine and β,γ-methyleneadenosine...

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
Share to Hydrogen-Ion Concentration

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

Share to Models, Molecular

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Sequence Alignment

Share to Thermus thermophilus

Source

Identifiers

PMID: 26510656
DOI: 10.1007/s10930-015-9636-8

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

Structural and Biochemical Studies on the Reaction Mechanism of Uridine-Cytidine Kinase.PMID 26510656Read ↗

Structural studies of a hyperthermophilic thymidylate kinase enzyme reveal conformational substates along the reaction coordinate.Semantic proximity Read ↗

Thymidylate Kinase: An Old Topic Brings New PerspectivesSemantic proximity Read ↗

Structural changes induced by ligand binding drastically increase the thermostability of the Ser/Thr protein kinase TpkD from Thermus thermophilus HB8.Semantic proximity Read ↗

Structure-function relationships of the ADP/ATP carrier.Semantic proximity Read ↗

Extending thymidine kinase activity to the catalytic repertoire of human deoxycytidine kinase.Semantic proximity Read ↗

The role of protein dynamics in thymidylate synthase catalysis: variants of conserved 2'-deoxyuridine 5'-monophosphate (dUMP)-binding Tyr-261.Semantic proximity Read ↗

Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes.Semantic proximity Read ↗

Specificity and catalysis of uracil DNA glycosylase. A molecular dynamics study of reactant and product complexes with DNA.Semantic proximity Read ↗

A template for the protein kinase family.Semantic proximity Read ↗

Structure of a type II thymidine kinase with bound dTTPSemantic proximity Read ↗

Functional groups required for the stability of yeast RNA triphosphatase in vitro and in vivo.Semantic proximity Read ↗

Mutational analyses of yeast RNA triphosphatases highlight a common mechanism of metal-dependent NTP hydrolysis and a means of targeting enzymes to pre-mRNAs in vivo by fusion to the guanylyltransferase component of the capping apparatus.Semantic proximity Read ↗

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