ArticleMolecular genetics and metabolism2009
N- and C-terminal domains in human holocarboxylase synthetase participate in substrate recognition.
Article in Molecular genetics and metabolism, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Hydrogen-Deuterium Exchange Defines Ligand-Induced Conformational Changes to the Class III Biotin Protein Ligase from Saccharomyces cerevisiae.Chembiochem : a European journal of chemical biology · 2025Article
- Dynamics, chemistry, and modeling studies in the aviation and aerospace transition zone.Innovation (Cambridge (Mass.)) · 2025Review
- The mitochondrial carboxylase PCCA interacts withApplied and environmental microbiology · 2024Article
- Analysis of the relationship between phenotypes and genotypes in 60 Chinese patients with propionic acidemia: a fourteen-year experience at a tertiary hospital.Orphanet journal of rare diseases · 2022Article
- Propionyl-CoA carboxylase - A review.Molecular genetics and metabolism · 2017Review
- Biotin: From Nutrition to Therapeutics.The Journal of nutrition · 2017Review
- Resveratrol compounds inhibit human holocarboxylase synthetase and cause a lean phenotype in Drosophila melanogaster.The Journal of nutritional biochemistry · 2015Article
- β-Keto and β-hydroxyphosphonate analogs of biotin-5'-AMP are inhibitors of holocarboxylase synthetase.Bioorganic & medicinal chemistry letters · 2014Article
- Holocarboxylase synthetase interacts physically with nuclear receptor co-repressor, histone deacetylase 1 and a novel splicing variant of histone deacetylase 1 to repress repeats.The Biochemical journal · 2014Article
- Novel roles of holocarboxylase synthetase in gene regulation and intermediary metabolism.Nutrition reviews · 2014Review
- Holocarboxylase synthetase interacts physically with euchromatic histone-lysine N-methyltransferase, linking histone biotinylation with methylation events.The Journal of nutritional biochemistry · 2013Article
- Structural characterization of Staphylococcus aureus biotin protein ligase and interaction partners: an antibiotic target.Protein science : a publication of the Protein Society · 2013Article
- Effects of single-nucleotide polymorphisms in the human holocarboxylase synthetase gene on enzyme catalysis.European journal of human genetics : EJHG · 2012Article
- A novel molecular mechanism to explain biotin-unresponsive holocarboxylase synthetase deficiency.Journal of molecular medicine (Berlin, Germany) · 2012Article
- Human holocarboxylase synthetase with a start site at methionine-58 is the predominant nuclear variant of this protein and has catalytic activity.Biochemical and biophysical research communications · 2011Article
- Holocarboxylase synthetase is a chromatin protein and interacts directly with histone H3 to mediate biotinylation of K9 and K18.The Journal of nutritional biochemistry · 2011Article
- The polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylation.Archives of biochemistry and biophysics · 2010Article
- Repression of transposable elements by histone biotinylation.The Journal of nutrition · 2009Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Holocarboxylase synthetase (HCS) catalyzes the binding of the vitamin biotin to carboxylases and histones. Carboxylases mediate essential steps in macronutrient metabolism. For example, propionyl-CoA carboxylase (PCC) catalyzes the carboxylation of propionyl-CoA in the metabolism of odd-chain fatty acids. HCS comprises four putative domains, i.e., the N-terminus, the biotin transfer/ATP-binding domain, a putative linker domain, and the C-terminus. Both N- and C-termini are essential for biotinylation of carboxylases by HCS, but the exact functions of these two domains in enzyme catalysis are unknown. Here we tested the hypothesis that N- and C-termini play roles in substrate recognition by HCS. Yeast-two-hybrid (Y2H) assays were used to study interactions between the four domains of human HCS with p67, a PCC-based polypeptide and HCS substrate. Both N- and C-termini interacted with p67 in Y2H assays, whereas the biotin transfer/ATP-binding and the linker domains did not interact with p67. The essentiality of N- and C-termini for interactions with carboxylases was confirmed in rescue experiments with mutant Saccharomyces cerevisiae, using constructs of truncated human HCS. Finally, a computational biology approach was used to model the 3D structure of human HCS and identify amino acid residues that interact with p67. In silico predictions were consistent with observations from Y2H assays and yeast rescue experiments, and suggested docking of p67 near Arg508 and Ser515 within the central domain of HCS.
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