Crystallization and preliminary crystallographic studies of the recombinant L-N-carbamoylase from Geobacillus stearothermophilus CECT43.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 64(Pt 12): 1135-8, 2008 Dec 01.
Article
em En
| MEDLINE
| ID: mdl-19052368
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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Base de dados:
MEDLINE
Assunto principal:
Geobacillus stearothermophilus
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Proteínas de Bactérias
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Amidoidrolases
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article