ArticleJournal of bacteriology2012
Mutational and structural analysis of L-N-carbamoylase reveals new insights into a peptidase M20/M25/M40 family member.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Endo-β-1,4-Xylanase GH10 fromInternational journal of molecular sciences · 2026Article
- Exploring the Kinetics and Thermodynamics of a Novel Histidine Ammonia-Lyase fromInternational journal of molecular sciences · 2024Article
- Structural and biochemical characterisation of the N-carbamoyl-β-alanine amidohydrolase from Rhizobium radiobacter MDC 8606.The FEBS journal · 2023Article
- Open Issues for Protein Function Assignment inGenes · 2021Article
- A fundamental catalytic difference between zinc and manganese dependent enzymes revealed in a bacterial isatin hydrolase.Scientific reports · 2018Article
- Enzymatic hydrolysis by transition-metal-dependent nucleophilic aromatic substitution.Nature chemical biology · 2016Article
- Identification of differentially expressed proteins from Leishmania amazonensis associated with the loss of virulence of the parasites.PLoS neglected tropical diseases · 2014Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-Carbamoyl-L-amino acid amidohydrolases (L-carbamoylases) are important industrial enzymes used in kinetic resolution of racemic mixtures of N-carbamoyl-amino acids due to their strict enantiospecificity. In this work, we report the first L-carbamoylase structure belonging to Geobacillus stearothermophilus CECT43 (BsLcar), at a resolution of 2.7 Å. Structural analysis of BsLcar and several members of the peptidase M20/M25/M40 family confirmed the expected conserved residues at the active site in this family, and site-directed mutagenesis revealed their relevance to substrate binding. We also found an unexpectedly conserved arginine residue (Arg(234) in BsLcar), proven to be critical for dimerization of the enzyme. The mutation of this sole residue resulted in a total loss of activity and prevented the formation of the dimer in BsLcar. Comparative studies revealed that the dimerization domain of the peptidase M20/M25/M40 family is a "small-molecule binding domain," allowing further evolutionary considerations for this enzyme family.
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