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

The molecular basis of ornithine transcarbamylase deficiency: modelling the human enzyme and the effects of mutations.

Journal of medical genetics - 1 Sept 1995

Tuchman M, Morizono H, Reish O, Yuan X, Allewell N M

Abstract excerpt

Human ornithine transcarbamylase is a trimer with 46% amino acid sequence homology to the catalytic subunit of E coli aspartate transcarbamylase. Secondary structure predictions, distributions of hydrophilic and hydrophobic regions, and the pattern of conserved residues suggest that the three dimensional structures of the two proteins are likely to be similar. A three dimensional model of ornithine...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites
Share to Escherichia coli

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Infant, Newborn

Share to Molecular Sequence Data

Share to Mutation

Share to Phenotype

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 8544185
DOI: 10.1136/jmg.32.9.680
PMCID: PMC1051666

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

The molecular basis of ornithine transcarbamylase deficiency: modelling the human enzyme and the effects of mutations.PMID 8544185Read ↗

Mutation Study of Malaysian Patients with Ornithine Transcarbamylase Deficiency: Clinical, Molecular, and Bioinformatics Analyses of Two Novel Missense Mutations of the OTC Gene.Semantic proximity Read ↗

The biochemical and molecular spectrum of ornithine transcarbamylase deficiency.Semantic proximity Read ↗

Mutations and polymorphisms in the human ornithine transcarbamylase gene.Semantic proximity Read ↗

Expression, purification and kinetic characterization of wild-type human ornithine transcarbamylase and a recurrent mutant that produces 'late onset' hyperammonaemia.Semantic proximity Read ↗

The clinical, biochemical, and molecular spectrum of ornithine transcarbamylase deficiency.Semantic proximity Read ↗

Mutations and polymorphisms in the human ornithine transcarbamylase gene: mutation update addendum.Semantic proximity Read ↗

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

Genotype-Phenotype Correlations in Ornithine Transcarbamylase Deficiency: A Mutation Update.Semantic proximity Read ↗

'Late onset' ornithine transcarbamylase deficiency: function of three purified recombinant mutant enzymes.Semantic proximity Read ↗

Crystallization and preliminary X-ray crystallographic studies of wild-type human ornithine transcarbamylase and two naturally occurring mutants at position 277.Semantic proximity Read ↗

Mutations and polymorphisms in the human ornithine transcarbamylase (<i>OTC</i>) geneSemantic proximity Read ↗

Seven new mutations in the human ornithine transcarbamylase gene.Semantic proximity Read ↗

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