Document Detail

Crystallization and preliminary crystallographic studies of the recombinant L-N-carbamoylase from Geobacillus stearothermophilus CECT43.
MedLine Citation:
PMID:  19052368     Owner:  NLM     Status:  MEDLINE    
N-Carbamoyl-L-amino-acid amidohydrolases (L-N-carbamoylases; EC 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.
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:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-11-28
Journal Detail:
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:
Created Date:  2008-12-04     Completed Date:  2009-01-23     Revised Date:  2013-06-04    
Medline Journal Info:
Nlm Unique ID:  101226117     Medline TA:  Acta Crystallogr Sect F Struct Biol Cryst Commun     Country:  England    
Other Details:
Languages:  eng     Pagination:  1135-8     Citation Subset:  IM    
Departamento Química Física, Bioquímica y Química Inorgánica, Universidad de Almería, Almería, Spain.
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MeSH Terms
Amidohydrolases / chemistry*,  genetics,  isolation & purification
Bacterial Proteins / chemistry*,  genetics,  isolation & purification
Cloning, Molecular
Crystallography, X-Ray
Geobacillus stearothermophilus / enzymology*,  metabolism
Molecular Weight
Recombinant Proteins / chemistry,  genetics,  isolation & purification
Reg. No./Substance:
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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