ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008
Crystallization and preliminary crystallographic studies of the recombinant L-N-carbamoylase from Geobacillus stearothermophilus CECT43.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 6 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
- Mutational and structural analysis of L-N-carbamoylase reveals new insights into a peptidase M20/M25/M40 family member.Journal of bacteriology · 2012Article
Corrections and comments
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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-N-carbamoylases; EC 3.5.1.87) hydrolyze the carbon-nitrogen bond of the ureido group in N-carbamoyl-L-alpha-amino acids. These enzymes are commonly used in the production of optically pure natural and non-natural L-amino acids using the ;hydantoinase process'. Recombinant L-N-carbamoylase from Geobacillus stearothermophilus CECT43 has been expressed, purified and crystallized by hanging-drop vapour diffusion. X-ray data were collected to a resolution of 2.75 A. The crystals belonged to space group P2(1)2(1)2, with unit-cell parameters a = 103.2, b = 211.7, c = 43.1 A and two subunits in the asymmetric unit.
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