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

Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer.

The Journal of biological chemistry - 10 Aug 2001

Janiyani K, Bordelon T, Waldrop G L, Cronan J E

Abstract excerpt

Biotin carboxylase catalyzes the ATP-dependent carboxylation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase that catalyzes the first committed step in fatty acid synthesis. The Escherichia coli biotin carboxylase is readily isolated from the other components of the acetyl-CoA carboxylase complex such that enzymatic activity is retained. The three-dimensional structure of biotin...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Biotin
Share to Carbon-Nitrogen Ligases

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

Share to Catalysis

Share to Chromatography

Share to Dimerization

Share to Epitopes

Share to Models, Chemical

Source

Identifiers

PMID: 11390406
DOI: 10.1074/jbc.M104102200

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

Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer.PMID 11390406Read ↗

Modeling and numerical simulation of biotin carboxylase kinetics: implications for half-sites reactivity.Semantic proximity Read ↗

Dimerization of the bacterial biotin carboxylase subunit is required for acetyl coenzyme A carboxylase activity in vivo.Semantic proximity Read ↗

The biotinyl domain of Escherichia coli acetyl-CoA carboxylase. Evidence that the "thumb" structure id essential and that the domain functions as a dimer.Semantic proximity Read ↗

Domain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzyme.Semantic proximity Read ↗

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

The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity.Semantic proximity Read ↗

Promiscuous protein biotinylation by Escherichia coli biotin protein ligase.Semantic proximity Read ↗

Crystal structure of the 500-kDa yeast acetyl-CoA carboxylase holoenzyme dimer.Semantic proximity Read ↗

A distinct holoenzyme organization for two-subunit pyruvate carboxylase.Semantic proximity Read ↗

Targeted and proximity-dependent promiscuous protein biotinylation by a mutant Escherichia coli biotin protein ligase.Semantic proximity Read ↗

Function of a conserved sequence motif in biotin holoenzyme synthetases.Semantic proximity Read ↗

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

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