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

Variants of human dihydrofolate reductase with substitutions at leucine-22: effect on catalytic and inhibitor binding properties.

Molecular pharmacology - 1 Mar 1996

Ercikan-Abali E A, Waltham M C, Dicker A P, Schweitzer B I, Gritsman H, Banerjee D, Bertino J R

Abstract excerpt

We investigated the enzyme kinetic and antifolate inhibitory properties of human dihydrofolate reductase enzyme with mutations at position 22. Leu-22 was changed to isoleucine, methionine, phenylalanine, and tyrosine to generate the various mutant enzymes. The overall catalytic efficiency (kcat/Km) for methionine and phenylalanine mutants was reduced approximately 3-fold and >6-fold for isoleucine and tyrosine...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Cells, Cultured

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

Share to Cricetinae

Share to Genetic Variation

Share to Kinetics

Share to Molecular Sequence Data

Share to Mutagenesis

Share to Mutation

Source

Identifiers

PMID: 8643082

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

Variants of human dihydrofolate reductase with substitutions at leucine-22: effect on catalytic and inhibitor binding properties.PMID 8643082Read ↗

Methotrexate-resistant variants of human dihydrofolate reductase with substitutions of leucine 22. Kinetics, crystallography, and potential as selectable markers.Semantic proximity Read ↗

Identification of amino acids required for the functional up-regulation of human dihydrofolate reductase protein in response to antifolate Treatment.Semantic proximity Read ↗

Mutations of human dihydrofolate reductase causing decreased inhibition by methotrexate.Semantic proximity Read ↗

Active site-directed double mutants of dihydrofolate reductase.Semantic proximity Read ↗

Methotrexate-resistant variants of human dihydrofolate reductase. Effects of Phe31 substitutions.Semantic proximity Read ↗

Increasing methotrexate resistance by combination of active-site mutations in human dihydrofolate reductase.Semantic proximity Read ↗

A miR-24 microRNA binding-site polymorphism in dihydrofolate reductase gene leads to methotrexate resistance.Semantic proximity Read ↗

Role of the conserved active site residue tryptophan-24 of human dihydrofolate reductase as revealed by mutagenesis.Semantic proximity Read ↗

The importance of loop region residues 40-46 in human dihydrofolate reductase as revealed by site-directed mutagenesis.Semantic proximity Read ↗

Mutational analysis of Plasmodium falciparum dihydrofolate reductase: the role of aspartate 54 and phenylalanine 223 on catalytic activity and antifolate binding.Semantic proximity Read ↗

Substrate and inhibitor specificity of Mycobacterium avium dihydrofolate reductase.Semantic proximity Read ↗

Comparison of the protection of cells from antifolates by transduced human dihydrofolate reductase mutants.Semantic proximity Read ↗

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