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

Functional characterization of PCCA mutations causing propionic acidemia.

Biochimica et biophysica acta - 20 Nov 2002

Clavero Sonia, Martínez Maria Angeles, Pérez Belén, Pérez-Cerdá Celia, Ugarte Magdalena, Desviat Lourdes R

Abstract excerpt

Propionic acidemia (PA, MIM 232000 and 232050) is caused by a deficiency of mitochondrial biotin-dependent propionyl-CoA carboxylase (PCC, EC 6.4.1.3), a heteropolymeric enzyme composed of alpha and beta subunits, which are encoded by the PCCA and PCCB genes, respectively. The PCCA protein (alpha subunit) is responsible for the formation of carboxybiotin upon hydrolysis of ATP and contains a C-terminal...

Read the complete abstract on PubMed

Topics

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

Share to Carbon-Carbon Ligases
Share to Cell-Free System

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

Share to DNA, Complementary

Share to Fibroblasts

Share to Mitochondria

Share to Mitochondria, Liver

Share to Propionates

Share to Protein Precursors

Source

Identifiers

PMID: 12385775
DOI: 10.1016/s0925-4439(02)00155-2

Genes

PCCA
PCCB

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

Functional characterization of PCCA mutations causing propionic acidemia.PMID 12385775Read ↗

Propionic acidemia: analysis of mutant propionyl-CoA carboxylase enzymes expressed in Escherichia coli.Semantic proximity Read ↗

Propionic acidemia: identification of twenty-four novel mutations in Europe and North America.Semantic proximity Read ↗

Functional analysis of PCCB mutations causing propionic acidemia based on expression studies in deficient human skin fibroblasts.Semantic proximity Read ↗

Propionic acidemia: mutation update and functional and structural effects of the variant alleles.Semantic proximity Read ↗

Structure of the PCCA gene and distribution of mutations causing propionic acidemia.Semantic proximity Read ↗

Changes in the carboxyl terminus of the beta subunit of human propionyl-CoA carboxylase affect the oligomer assembly and catalysis: expression and characterization of seven patient-derived mutant forms of PCC in Escherichia coli.Semantic proximity Read ↗

Coding sequence mutations in the alpha subunit of propionyl-CoA carboxylase in patients with propionic acidemia.Semantic proximity Read ↗

Functional characterization of novel genotypes and cellular oxidative stress studies in propionic acidemia.Semantic proximity Read ↗

Human propionyl-CoA carboxylase beta subunit gene: exon-intron definition and mutation spectrum in Spanish and Latin American propionic acidemia patients.Semantic proximity Read ↗

Overview of mutations in the PCCA and PCCB genes causing propionic acidemia.Semantic proximity Read ↗

Characterization of four variant forms of human propionyl-CoA carboxylase expressed in Escherichia coli.Semantic proximity Read ↗

Three novel splice mutations in the PCCA gene causing identical exon skipping in propionic acidemia patients.Semantic proximity Read ↗

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