ArticleThe Journal of biological chemistry2011
Biotinylation, a post-translational modification controlled by the rate of protein-protein association.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- The effects of chemotherapy on brain regions: implications for chemobrain revealed through metabolomic profiling.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Simultaneous profiling of native-state proteomes and transcriptomes of neural cell types using proximity labeling.Nature communications · 2026Article
- 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
- Specificity and selectivity in post-translational biotin addition.Biochemical Society transactions · 2018Review
- Protein:protein interactions in control of a transcriptional switch.Journal of molecular biology · 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
- Modified recombinant proteins can be exported via the Sec pathway in Escherichia coli.PloS one · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Biotin protein ligases catalyze specific covalent linkage of the coenzyme biotin to biotin-dependent carboxylases. The reaction proceeds in two steps, including synthesis of an adenylated intermediate followed by biotin transfer to the carboxylase substrate. In this work specificity in the transfer reaction was investigated using single turnover stopped-flow and quench-flow assays. Cognate and noncognate reactions were measured using the enzymes and minimal biotin acceptor substrates from Escherichia coli, Pyrococcus horikoshii, and Homo sapiens. The kinetic analysis demonstrates that for all enzyme-substrate pairs the bimolecular rate of association of enzyme with substrate limits post-translational biotinylation. In addition, in noncognate reactions the three enzymes displayed a range of selectivities. These results highlight the importance of protein-protein binding kinetics for specific biotin addition to carboxylases and provide one mechanism for determining biotin distribution in metabolism.
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Registered trials
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