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

Disruption of the crossover helix impairs dihydrofolate reductase activity in the bifunctional enzyme TS-DHFR from Cryptosporidium hominis.

The Biochemical journal - 1 Feb 2009

Vargo Melissa A, Martucci W Edward, Anderson Karen S

Abstract excerpt

In contrast with most species, including humans, which have monofunctional forms of the folate biosynthetic enzymes TS (thymidylate synthase) and DHFR (dihydrofolate reductase), several pathogenic protozoal parasites, including Cryptosporidium hominis, contain a bifunctional form of the enzymes on a single polypeptide chain having both catalytic activities. The crystal structure of the bifunctional enzyme TS-DHFR...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Catalytic Domain
Share to Cryptosporidium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Multienzyme Complexes

Share to Protozoan Proteins

Share to Tetrahydrofolate Dehydrogenase

Share to Thymidylate Synthase

Source

Open in PubMed Open full text

Identifiers

PMID: 18851711
DOI: 10.1042/BJ20081247
PMCID: PMC2769570

Genes

DHFR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Disruption of the crossover helix impairs dihydrofolate reductase activity in the bifunctional enzyme TS-DHFR from Cryptosporidium hominis.PMID 18851711Read ↗

First Three-Dimensional Structure of <i>Toxoplasma gondii</i> Thymidylate Synthase–Dihydrofolate Reductase: Insights for Catalysis, Interdomain Interactions, and Substrate ChannelingSemantic proximity Read ↗

Explaining an unusually fast parasitic enzyme: folate tail-binding residues dictate substrate positioning and catalysis in Cryptosporidium hominis thymidylate synthase.Semantic proximity Read ↗

Mutational 'hot-spots' in mammalian, bacterial and protozoal dihydrofolate reductases associated with antifolate resistance: sequence and structural comparison.Semantic proximity Read ↗

Divergent evolution of protein conformational dynamics in dihydrofolate reductase.Semantic proximity Read ↗

Structural Comparison of Enterococcus faecalis and Human Thymidylate Synthase Complexes with the Substrate dUMP and Its Analogue FdUMP Provides Hints about Enzyme Conformational VariabilitiesSemantic proximity Read ↗

Bifunctional thymidylate synthase‐dihydrofolate reductase in protozoaSemantic proximity Read ↗

A Kinetic Alignment of Orthologous Inosine-5′-monophosphate DehydrogenasesSemantic proximity Read ↗

The structure of<i>Enterococcus faecalis</i>thymidylate synthase provides clues about folate bacterial metabolismSemantic proximity Read ↗

Specific glycine-dependent enzyme motion determines the potency of conformation selective inhibitors of threonyl-tRNA synthetase.Semantic proximity Read ↗

Formation of catalytically active cross-species heterodimers of thymidylate synthase from Plasmodium falciparum and Plasmodium vivax.Semantic proximity Read ↗

Kinetic and structural characterization of dihydrofolate reductase from Streptococcus pneumoniae.Semantic proximity Read ↗

Conferring a template-dependent polymerase activity to terminal deoxynucleotidyltransferase by mutations in the Loop1 region.Semantic proximity Read ↗

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