ArticleThe Journal of biological chemistry2009
Distinct amino termini of two human HCS isoforms influence biotin acceptor substrate recognition.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 26 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
- A comprehensive approach for detection of biotin deficiency from dried blood spot samples using liquid chromatography-mass spectrometry.Future science OA · 2024Article
- Biotin protein ligase as you like it: Either extraordinarily specific or promiscuous protein biotinylation.Proteins · 2024Review
- Specificity and selectivity in post-translational biotin addition.Biochemical Society transactions · 2018Review
- A conserved regulatory mechanism in bifunctional biotin protein ligases.Protein science : a publication of the Protein Society · 2017Article
- 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
- Structural characterization of Staphylococcus aureus biotin protein ligase and interaction partners: an antibiotic target.Protein science : a publication of the Protein Society · 2013Article
- Functional versatility of a single protein surface in two protein:protein interactions.Journal of molecular biology · 2012Article
- Selectivity in post-translational biotin addition to five human carboxylases.The Journal of biological chemistry · 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
- Biotinylation, a post-translational modification controlled by the rate of protein-protein association.The Journal of biological chemistry · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The human holocarboxylase synthetase (HCS) catalyzes transfer of biotin to biotin-dependent carboxylases, and the enzyme is therefore of fundamental importance for many physiological processes, including fatty acid synthesis, gluconeogenesis, and amino acid catabolism. In addition, the enzyme functions in regulating transcription initiation at several genes that code for proteins involved in biotin metabolism. Two major forms of HCS exist in humans, which differ at the amino terminus by 57 amino acids. In this work, the two proteins were expressed in Escherichia coli, purified, and subjected to biochemical characterization. Equilibrium sedimentation indicates that the two proteins are monomers both in their apo-forms and when bound to the enzymatic intermediate biotinyl 5'-AMP. Steady state kinetic analyses as a function of biotin, ATP, or a minimal biotin-accepting substrate concentration indicate similar behaviors for both isoforms. However, pre-steady state analysis of biotin transfer reveals that the full-length HCS associates with the minimal biotin acceptor substrate with a rate twice as fast as that of the truncated isoform. These results are consistent with a role for the HCS amino terminus in biotin acceptor substrate recognition.
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