| Crystallization and preliminary crystallographic studies of the recombinant L-N-carbamoylase from Geobacillus stearothermophilus CECT43. | |
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MedLine Citation:
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PMID: 19052368 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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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Authors:
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Sergio Martínez-Rodríguez; Abel García-Pino; Francisco Javier Las Heras-Vázquez; Josefa María Clemente-Jiménez; Felipe Rodríguez-Vico; Remy Loris; Juan Ma García-Ruiz; Jose Antonio Gavira |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2008-11-28 |
Journal Detail:
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Title: Acta crystallographica. Section F, Structural biology and crystallization communications Volume: 64 ISSN: 1744-3091 ISO Abbreviation: Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. Publication Date: 2008 Dec |
Date Detail:
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Created Date: 2008-12-04 Completed Date: 2009-01-23 Revised Date: 2011-03-03 |
Medline Journal Info:
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Nlm Unique ID: 101226117 Medline TA: Acta Crystallogr Sect F Struct Biol Cryst Commun Country: England |
Other Details:
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Languages: eng Pagination: 1135-8 Citation Subset: IM |
Affiliation:
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Departamento Química Física, Bioquímica y Química Inorgánica, Universidad de Almería, Almería, Spain. srodrig@ual.es |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amidohydrolases
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chemistry*,
genetics,
isolation & purification Bacterial Proteins / chemistry*, genetics, isolation & purification Cloning, Molecular Crystallization Crystallography, X-Ray Geobacillus stearothermophilus / enzymology*, metabolism Molecular Weight Recombinant Proteins / chemistry, genetics, isolation & purification |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Recombinant Proteins; EC 3.5.-/Amidohydrolases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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