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 N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein.

FEBS letters - 19 Feb 2010

Lee Chung-Kyung, Cheong Chaejoon, Jeon Young Ho

Abstract excerpt

Human holocarboxylase synthetase shows a high degree of sequence homology in the catalytic domain with bacterial biotin ligases such as Escherichia coli BirA, but differs in the length and sequence of the N-terminus. Despite several studies having been undertaken on the N-terminal region of hHCS,...

Read the complete abstract on PubMed

Topics

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

Share to Biotinylation
Share to Carbon-Nitrogen Ligases
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chymotrypsin

Share to Circular Dichroism

Share to Electrophoresis, Polyacrylamide Gel

Share to Endopeptidase K

Share to Magnetic Resonance Spectroscopy

Source

Identifiers

PMID: 20085763
DOI: 10.1016/j.febslet.2009.12.059

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20085763-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein.PMID 20085763Read ↗

The polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylation.Semantic proximity Read ↗

The role of holocarboxylase synthetase in genome stability is mediated partly by epigenomic synergies between methylation and biotinylation events.Semantic proximity Read ↗

Effects of single-nucleotide polymorphisms in the human holocarboxylase synthetase gene on enzyme catalysis.Semantic proximity Read ↗

Clinical findings and biochemical and molecular analysis of four patients with holocarboxylase synthetase deficiency.Semantic proximity Read ↗

Late-onset holocarboxylase synthetase deficiency with homologous R508W mutation.Semantic proximity Read ↗

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

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

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

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

Structure of human holocarboxylase synthetase gene and mutation spectrum of holocarboxylase synthetase deficiency.Semantic proximity Read ↗

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

Holocarboxylase synthetase is an obligate participant in biotin-mediated regulation of its own expression and of biotin-dependent carboxylases mRNA levels in human cells.Semantic proximity Read ↗

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