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

Current Insight into Human Ornithine Aminotransferase: A Review.

Proteins - 1 Aug 2026

Floriani Fulvio, Borri Voltattorni Carla, Montioli Riccardo

Abstract excerpt

Human ornithine aminotransferase (hOAT) is a mitochondrial matrix pyridoxal-5'-phosphate enzyme (PLP) that catalyzes the reversible transfer of the δ-amino group of L-ornithine (L-Orn) to α-ketoglutarate (α-KG) yielding glutamate-5-semialdehyde (GSA) and glutamate. GSA is prone to cyclize to Δ1-pyrroline-5-carboxylate. Human OAT holds significant clinical and scientific interest because (i) its dysfunction causes...

Read the complete abstract on PubMed

Topics

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

Share to Catalytic Domain
Share to OAT gene
Share to Kinetics

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

Share to Models, Molecular

Share to Mutation

Share to Ornithine

Share to Recombinant Proteins

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 41887919
DOI: 10.1002/prot.70134
PMCID: PMC13327489

Genes

OAT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 25 Oct 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

Current Insight into Human Ornithine Aminotransferase: A Review.PMID 41887919Read ↗

Deficit of human ornithine aminotransferase in gyrate atrophy: Molecular, cellular, and clinical aspects.Semantic proximity Read ↗

Biochemical and Bioinformatic Studies of Mutations of Residues at the Monomer-Monomer Interface of Human Ornithine Aminotransferase Leading to Gyrate Atrophy of Choroid and Retina.Semantic proximity Read ↗

Extending diagnostic practices in gyrate atrophy: Enzymatic characterization and the development of an in vitro pyridoxine responsiveness assay.Semantic proximity Read ↗

Three novel mutations of the ornithine aminotransferase (OAT) gene in gyrate atrophy.Semantic proximity Read ↗

First report of c.425-1G>A mutation in ornithine aminotransferase gene causing gyrate atrophy of the choroid and retina with hyperornithinemia.Semantic proximity Read ↗

Finnish gyrate atrophy mutation OAT;c.1205C>T leads to accumulation of intracellular GABASemantic proximity Read ↗

Ornithine delta-aminotransferase mutations in gyrate atrophy. Allelic heterogeneity and functional consequences.Semantic proximity Read ↗

Determinants of substrate specificity in omega-aminotransferases.Semantic proximity Read ↗

Structural and functional analysis of mutations in alkaptonuria.Semantic proximity Read ↗

Functional analysis of missense mutations of OAT, causing gyrate atrophy of choroid and retina.Semantic proximity Read ↗

Variable phenotypes of gyrate atrophy in siblings with a nonsense mutation in OAT gene.Semantic proximity Read ↗

Biochemical Characterization of Disease-Associated Variants of Human Ornithine Transcarbamylase.Semantic proximity Read ↗

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