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

Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: evidence for cooperativity in biotin carboxylase.

The Journal of biological chemistry - 16 Apr 2004

Sloane Valerie, Waldrop Grover L

Abstract excerpt

Acetyl-CoA carboxylase catalyzes the committed step in fatty acid synthesis in all plants, animals, and bacteria. The Escherichia coli form is a multifunctional enzyme consisting of three separate proteins: biotin carboxylase, carboxyltransferase, and the biotin carboxyl carrier protein. The biotin carboxylase component, which catalyzes the ATP-dependent carboxylation of biotin using bicarbonate as the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Metabolism, Inborn Errors
Share to Biotin

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

Share to Carbon-Nitrogen Ligases

Share to Catalysis

Share to Crystallography, X-Ray

Share to Mutagenesis, Site-Directed

Share to Structure-Activity Relationship

Share to Substrate Specificity

Source

Identifiers

PMID: 14960587
DOI: 10.1074/jbc.M311982200

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

Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: evidence for cooperativity in biotin carboxylase.PMID 14960587Read ↗

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

Functional characterization of PCCA 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 ↗

The utility of molecular dynamics simulations for understanding site-directed mutagenesis of glycine residues in biotin carboxylase.Semantic proximity Read ↗

Relationship between kinetic properties of mutant enzyme and biochemical and clinical responsiveness to biotin in holocarboxylase synthetase deficiency.Semantic proximity Read ↗

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

Analysis of mutations causing biotinidase deficiency.Semantic proximity Read ↗

Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer.Semantic proximity Read ↗

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

Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase.Semantic proximity Read ↗

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

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

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