Open AccessCrystallization and preliminary crystallographic studies of the recombinant l ‐ N ‐carbamoylase from Geobacillus stearothermophilus CECT43
Author(s) -
MartínezRodríguez Sergio,
GarcíaPino Abel,
Las HerasVázquez Francisco Javier,
ClementeJiménez Josefa María,
RodríguezVico Felipe,
Loris Remy,
GarcíaRuiz Juan Ma.,
Gavira Jose Antonio
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108034830
Subject(s) - geobacillus stearothermophilus , crystallization , hydrolysis , recombinant dna , amino acid , chemistry , enzyme , stereochemistry , crystallography , biochemistry , thermophile , organic chemistry , gene
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 ‐α‐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 Å. The crystals belonged to space group P 2 1 2 1 2, with unit‐cell parameters a = 103.2, b = 211.7, c = 43.1 Å and two subunits in the asymmetric unit.