Crystallization and preliminary X-ray diffraction studies of monomeric isocitrate dehydrogenase from Corynebacterium glutamicum.
A monomeric isocitrate dehydrogenase has been crystallized for the first time. This enzyme catalyzes the conversion of isocitrate to oxalosuccinate and subsequently to alpha-ketoglutarate and CO(2); the coenzyme NADP(+) is reduced to NADPH during the reaction. Polyethylene glycol 2000 monomethyl ether was used to crystallize the enzyme in space group C2 with unit-cell parameters a = 137.1, b = 54.6, c = 126.4 A, beta = 108.2 degrees. The very small crystal (0. 05 x 0.20 x 0.05 mm) diffracted to 3.5 A d spacing using synchrotron radiation.
Audette
G F
GF
Department of Biochemistry, University of Saskatchewan, 107 Wiggins Road, Saskatoon SK, S7K 5E5, Canada.
Quail
J W
JW
Hayakawa
K
K
Bai
C
C
Chen
R
R
Delbaere
L T
LT
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D003352:Corynebacterium / Q000201:enzymology*; D003460:Crystallization; D019281:Dimerization; D007521:Isocitrate Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D007521:Isocitrate Dehydrogenase; C039355:isocitrate dehydrogenase (NADP+)