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

Identification of unique amino acids that modulate CYP4A7 activity.

Biochemistry - 12 Dec 2000

Loughran P A, Roman L J, Aitken A E, Miller R T, Masters B S

Abstract excerpt

A multifamily sequence alignment of the rabbit CYP4A members with the known structure of CYP102 indicates amino acid differences falling within the so-called substrate recognition site(s) (SRS). Chimeric proteins constructed between CYP4A4 and CYP4A7 indicate that laurate activity is affected by the residues within SRS1 and prostaglandin activity is influenced by SRS2-3. Site-directed mutant proteins of CYP4A7...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Arachidonic Acid
Share to Cytochrome P-450 Enzyme System

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

Share to Mixed Function Oxygenases

Share to Mutagenesis, Site-Directed

Share to Rabbits

Share to Sequence Alignment

Share to Substrate Specificity

Source

Identifiers

PMID: 11106489
DOI: 10.1021/bi001522u

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

Identification of unique amino acids that modulate CYP4A7 activity.PMID 11106489Read ↗

Biochemical analysis of recombinant CYP4A11 allelic variant enzymes: W126R, K276T and S353G.Semantic proximity Read ↗

Acyl-coenzyme A:cholesterol acyltransferase 1 - significance of single-nucleotide polymorphism at residue 526 and the role of Pro347 near the fifth transmembrane domain.Semantic proximity Read ↗

Folding requirements are different between sterol 14alpha-demethylase (CYP51) from Mycobacterium tuberculosis and human or fungal orthologs.Semantic proximity Read ↗

Amino acid differences in the deduced 5-lipoxygenase sequence of CAST atherosclerosis-resistance mice confer impaired activity when introduced into the human ortholog.Semantic proximity Read ↗

The catalytic architecture of leukotriene C4 synthase with two arginine residues.Semantic proximity Read ↗

Structure-function relationships of rat liver CYP3A9 to its human liver orthologs: site-directed active site mutagenesis to a progesterone dihydroxylase.Semantic proximity Read ↗

Identification of universal selectivity-determining positions in cytochrome P450 monooxygenases by systematic sequence-based literature mining.Semantic proximity Read ↗

The catalytic site of cytochrome P4504A11 (CYP4A11) and its L131F mutant.Semantic proximity Read ↗

The N-terminus of COX-1 and its effect on cyclooxygenase-1 catalytic activity.Semantic proximity Read ↗

Construction of a catalytically inactive cholesterol oxidase mutant: investigation of the interplay between active site-residues glutamate 361 and histidine 447.Semantic proximity Read ↗

Structure and phospholipase function of peroxiredoxin 6: identification of the catalytic triad and its role in phospholipid substrate binding.Semantic proximity Read ↗

Human platelet 12-lipoxygenase: naturally occurring Q261/R261 variants and N544L mutant show altered activity but unaffected substrate binding and membrane association behavior.Semantic proximity Read ↗

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