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

Thermodynamic characterization of the binding of dCMP to the Asn229Asp mutant of thymidylate synthase.

FEBS letters - 16 Jun 1997

Téllez-Sanz R, Bernier-Villamor V, García-Fuentes L, González-Pacanowska D, Barón C

Abstract excerpt

Isothermal titration microcalorimetry and equilibrium dialysis have been used to characterize the binding of 2'-deoxycytidine 5'-monophosphate (dCMP) to the Asn229Asp mutant of Lactobacillus casei recombinant thymidylate synthase at pH 7.4 over a temperature range of 15 degrees C to 35 degrees C. Equilibrium dialysis analysis shows that dCMP binds to two sites in the dimer of both wild-type and mutant thymidylate...

Read the complete abstract on PubMed

Topics

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

Share to Asparagine
Share to Aspartic Acid
Share to Calorimetry

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Binding

Share to Temperature

Share to Thermodynamics

Share to Thymidylate Synthase

Source

Identifiers

PMID: 9224695
DOI: 10.1016/s0014-5793(97)00551-6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Thermodynamic characterization of the binding of dCMP to the Asn229Asp mutant of thymidylate synthase.PMID 9224695Read ↗

Mutation of asparagine 229 to aspartate in thymidylate synthase converts the enzyme to a deoxycytidylate methylase.Semantic proximity Read ↗

Effect of amino acid substitutions at the subunit interface on the stability and aggregation properties of a dimeric protein: role of Arg 178 and Arg 218 at the Dimer interface of thymidylate synthase.Semantic proximity Read ↗

Role of an invariant lysine residue in folate binding on Escherichia coli thymidylate synthase: calorimetric and crystallographic analysis of the K48Q mutant.Semantic proximity Read ↗

Exclusion of 2'-deoxycytidine 5'-monophosphate by asparagine 229 of thymidylate synthase.Semantic proximity Read ↗

Role of the conserved tryptophan 82 of Lactobacillus casei thymidylate synthase.Semantic proximity Read ↗

Partitioning roles of side chains in affinity, orientation, and catalysis with structures for mutant complexes: asparagine-229 in thymidylate synthase.Semantic proximity Read ↗

A double role for a strictly conserved serine: further insights into the dUTPase catalytic mechanism.Semantic proximity Read ↗

Bacterial versus human thymidylate synthase: Kinetics and functionalitySemantic proximity Read ↗

Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases.Semantic proximity Read ↗

Examination of the reduced affinity of the thymidylate synthase G52S mutation for FdUMP by ab initio and semi-empirical studies.Semantic proximity Read ↗

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

Widespread Perturbation of Function, Structure, and Dynamics by a Conservative Single-Atom Substitution in Thymidylate Synthase.Semantic proximity Read ↗

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