ArticleProtein science : a publication of the Protein Society2008
Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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45 citing papers in PubMed, 85 citations in OpenAlex.
- Catalytic loop closure governs substrate selectivity in the rhizocticin biosynthetic ligases RhiM and RhiC.The Journal of biological chemistry · 2026Article
- Oligomeric assemblies of plant biotin carboxylase revealed by cryo-EM and cross-linking.The Biochemical journal · 2026Article
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- Structural insight into synergistic activation of human 3-methylcrotonyl-CoA carboxylase.Nature structural & molecular biology · 2025Article
- Bioinformatics study of biotin carboxylase B-subdomain isolated fromBiotechnologia · 2025Article
- ActivebioRxiv : the preprint server for biology · 2024Article
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- Purification of heteromeric acetyl-CoA carboxylases from Escherichia coli for structure solution.Methods in enzymology · 2024Article
- In silico Analysis of Two Novel Variants in the Pyruvate Carboxylase (PC) Gene Associated with the Severe Form of PC Deficiency.Iranian biomedical journal · 2023Article
- Transmission and microevolution of methicillin-resistantFrontiers in public health · 2022Article
- The Classical, Yet Controversial, First Enzyme of Lipid Synthesis: Escherichia coli Acetyl-CoA Carboxylase.Microbiology and molecular biology reviews : MMBR · 2021Review
- Modified nucleoside triphosphates in bacterial research forRSC chemical biology · 2020Article
- Optimization and Mechanistic Characterization of Pyridopyrimidine Inhibitors of Bacterial Biotin Carboxylase.Journal of medicinal chemistry · 2019Article
- Quaternary structure of α-amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) controls its activity.The Journal of biological chemistry · 2019Article
- Status of Targeting MreB for the Development of Antibiotics.Frontiers in chemistry · 2019Review
- Crystal structure of the essential biotin-dependent carboxylase AccA3 fromFEBS open bio · 2017Article
- An engineered heterodimeric model to investigate SULT1B1 dependence on intersubunit communication.Biochemical pharmacology · 2016Article
- Article
- Structural Analysis of Substrate, Reaction Intermediate, and Product Binding in Haemophilus influenzae Biotin Carboxylase.Biochemistry · 2015Article
- Dimeric human sulfotransferase 1B1 displays cofactor-dependent subunit communication.Pharmacology research & perspectives · 2015Article
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7 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Bacterial acetyl-CoA carboxylase is a multifunctional biotin-dependent enzyme that consists of three separate proteins: biotin carboxylase (BC), biotin carboxyl carrier protein (BCCP), and carboxyltransferase (CT). Acetyl-CoA carboxylase is a potentially attractive target for novel antibiotics because it catalyzes the first committed step in fatty acid biosynthesis. In the first half-reaction, BC catalyzes the ATP-dependent carboxylation of BCCP. In the second half-reaction, the carboxyl group is transferred from carboxybiotinylated BCCP to acetyl-CoA to produce malonyl-CoA. A series of structures of BC from several bacteria crystallized in the presence of various ATP analogs is described that addresses three major questions concerning the catalytic mechanism. The structure of BC bound to AMPPNP and the two catalytically essential magnesium ions resolves inconsistencies between the kinetics of active-site BC mutants and previously reported BC structures. Another structure of AMPPNP bound to BC shows the polyphosphate chain folded back on itself, and not in the correct (i.e., extended) conformation for catalysis. This provides the first structural evidence for the hypothesis of substrate-induced synergism, which posits that ATP binds nonproductively to BC in the absence of biotin. The BC homodimer has been proposed to exhibit half-sites reactivity where the active sites alternate or "flip-flop" their catalytic cycles. A crystal structure of BC showed the ATP analog AMPPCF(2)P bound to one subunit while the other subunit was unliganded. The liganded subunit was in the closed or catalytic conformation while the unliganded subunit was in the open conformation. This provides the first structural evidence for half-sites reactivity in BC.
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