ArticleThe Journal of biological chemistry2012
Crystal structure of urea carboxylase provides insights into the carboxyltransfer reaction.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 42 citations in OpenAlex.
- Electroenzymatic COAngewandte Chemie (International ed. in English) · 2026Review
- Structural basis for substrate specificity and MSMEG_0435-0436 binding by the mycobacterial long-chain acyl-CoA carboxylase complex.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Viral infection collapses intracytoplasmic membrane integrity and autotrophic metabolism in ammonia-oxidizingISME communications · 2026Article
- Effect of biotin on growth performance, serum biochemical profiles, and histomorphological changes in acetate gossypol-treated mice.Frontiers in veterinary science · 2025Article
- Sample optimizations to enable the structure determination of biotin-dependent carboxylases.Methods in enzymology · 2024Article
- Enzymatic Conversion of COChemical reviews · 2023Review
- The opportunistic pathogen Pseudomonas aeruginosa exploits bacterial biotin synthesis pathway to benefit its infectivity.PLoS pathogens · 2023Article
- Solving the Conundrum: Widespread Proteins Annotated for Urea Metabolism in Bacteria Are Carboxyguanidine Deiminases Mediating Nitrogen Assimilation from Guanidine.Biochemistry · 2020Article
- Single-particle analysis of urea amidolyase reveals its molecular mechanism.Protein science : a publication of the Protein Society · 2020Article
- Kinetic, Structural, and Mutational Analysis of Acyl-CoA Carboxylase FromFrontiers in molecular biosciences · 2020Article
- Structure and function of urea amidolyase.Bioscience reports · 2018Article
- Metabolism of Free Guanidine in Bacteria Is Regulated by a Widespread Riboswitch Class.Molecular cell · 2017Article
- Amino Acids Are an Ineffective Fertilizer forFrontiers in plant science · 2017Article
- The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent.Protein science : a publication of the Protein Society · 2016Article
- A unified molecular mechanism for the regulation of acetyl-CoA carboxylase by phosphorylation.Cell discovery · 2016Article
- Structure and substrate selectivity of the 750-kDa α6β6 holoenzyme of geranyl-CoA carboxylase.Nature communications · 2015Article
- Article
- Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase.Nature · 2015Article
- Structure and function of allophanate hydrolase.The Journal of biological chemistry · 2013Article
- The three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase.Structure (London, England : 1993) · 2013Article
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Authors and funding
4 authors at 3 institutions in 3 countries.
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Abstract
Urea carboxylase (UC) is conserved in many bacteria, algae, and fungi and catalyzes the conversion of urea to allophanate, an essential step in the utilization of urea as a nitrogen source in these organisms. UC belongs to the biotin-dependent carboxylase superfamily and shares the biotin carboxylase (BC) and biotin carboxyl carrier protein (BCCP) domains with these other enzymes, but its carboxyltransferase (CT) domain is distinct. Currently, there is no information on the molecular basis of catalysis by UC. We report here the crystal structure of the Kluyveromyces lactis UC and biochemical studies to assess the structural information. Structural and sequence analyses indicate the CT domain of UC belongs to a large family of proteins with diverse functions, including the Bacillus subtilis KipA-KipI complex, which has important functions in sporulation regulation. A structure of the KipA-KipI complex is not currently available, and our structure provides a framework to understand the function of this complex. Most interestingly, in the structure the CT domain interacts with the BCCP domain, with biotin and a urea molecule bound at its active site. This structural information and our follow-up biochemical experiments provided molecular insights into the UC carboxyltransfer reaction. Several structural elements important for the UC carboxyltransfer reaction are found in other biotin-dependent carboxylases and might be conserved within this family, and our data could shed light on the mechanism of catalysis of these enzymes.
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