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 polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylation.

Archives of biochemistry and biophysics - 1 Mar 2010

Hassan Yousef I, Moriyama Hideaki, Zempleni Janos

Abstract excerpt

Holocarboxylase synthetase (HCS) catalyzes the binding of biotin to lysines in carboxylases and histones in two steps. First, HCS catalyzes the synthesis of biotinyl-5'-AMP; second, the biotinyl moiety is ligated to lysine residues. It has been proposed that step two is fairly promiscuous, and th...

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 Biotinylation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Carbon-Nitrogen Ligases

Share to Models, Molecular

Share to Mutagenesis, Site-Directed

Share to Peptides

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 20026029
DOI: 10.1016/j.abb.2009.12.017
PMCID: PMC2824026

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20026029-2026-09-02.2. 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 polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylation.PMID 20026029Read ↗

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

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

Protein post-translational modification by lysine succinylation: Biochemistry, biological implications, and therapeutic opportunitiesSemantic proximity Read ↗

Biotinylation is a natural, albeit rare, modification of human histonesSemantic proximity Read ↗

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

Susceptibility to heat stress and aberrant gene expression patterns in holocarboxylase synthetase-deficient Drosophila melanogaster are caused by decreased biotinylation of histones, not of carboxylases.Semantic proximity Read ↗

Biotinylation of lysine method identifies acetylated histone H3 lysine 79 in Saccharomyces cerevisiae as a substrate for Sir2.Semantic proximity Read ↗

Characterization of PROTAC specificity and endogenous protein interactomes using ProtacIDSemantic proximity Read ↗

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

Dehomocysteinylation is catalysed by the sirtuin-2-like bacterial lysine deacetylase CobB.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 ↗

The <i>E. coli</i> sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sitesSemantic proximity Read ↗

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