Preliminary X-ray crystallographic study of cyanase from Escherichia coli.
Cyanase, an oligomeric enzyme of Escherichia coli that catalyzes the decomposition of cyanate to ammonia and bicarbonate, crystallizes in the space group P1 with unit cell parameters a = 85.96 A, b = 83.17 A, c = 83.28 A, alpha = 110.29 degrees, beta = 118.29 degrees and gamma = 72.40 degrees. Crystals diffract to a resolution of at least 2.5 A. The crystal data, in conjunction with a subunit molecular weight of 17,008, suggest that two oligomers are in the asymmetric unit of the crystal and that eight subunits comprise a single oligomer.
Kim
K H
KH
Department of Biochemistry and Biophysics, Iowa State University, Ames 50011.
Honzatko
R B
RB
Little
R M
RM
Anderson
P M
PM
D000619:Aminohydrolases; D019759:Carbon-Nitrogen Lyases; D004926:Escherichia coli / Q000201:enzymology*; D008970:Molecular Weight; D014961:X-Ray Diffraction
D000619:Aminohydrolases; C019953:cyanate hydrolase; D019759:Carbon-Nitrogen Lyases