Crystallization and preliminary X-ray analysis of L-azetidine-2-carboxylate hydrolase from Pseudomonas sp. strain A2C.
L-Azetidine-2-carboxylate hydrolase from Pseudomonas sp. strain A2C catalyzes a ring-opening reaction that detoxifies L-azetidine-2-carboxylate, an analogue of L-proline. Recombinant L-azetidine-2-carboxylate hydrolase was overexpressed, purified and crystallized using polyethylene glycol and magnesium acetate as precipitants. The needle-shaped crystal belonged to space group P2(1), with unit-cell parameters a = 35.6, b = 63.6, c = 54.7 A, beta = 105.5 degrees . The crystal diffracted to a resolution of 1.38 A. The calculated V(M) value was 2.2 A(3) Da(-1), suggesting that the crystal contains one enzyme subunit in the asymmetric unit.
Toyoda
Mayuko
M
Laboratory of Molecular Microbial Science, Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Jitsumori
Keiji
K
Mikami
Bunzo
B
Wackett
Lawrence P
LP
Kurihara
Tatsuo
T
Esaki
Nobuyoshi
N
D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D006867:Hydrolases / Q000737:chemistry*; D008969:Molecular Sequence Data; D011549:Pseudomonas / Q000201:enzymology*; D016415:Sequence Alignment
D006867:Hydrolases