Crystallization and preliminary X-ray studies of a Bacillus subtilis and Thermus thermophilus HB8 chimeric 3-isopropylmalate dehydrogenase.
A chimeric gene was constructed by fusing the Bacillus subtilis and Thermus thermophilus genes coding for 3-isopropylmalate dehydrogenase, and expressed in Escherichia coli. The chimeric enzyme was crystallized in a size suitable for X-ray structure analysis. The crystal has a space group of P3(1)21 or P3(2)21, a = b = 77.1 A and c = 158.3 A, which is isomorphous with that of the native enzyme from T. thermophilus.
Onodera
K
K
Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Kanagawa.
Moriyama
H
H
Takenaka
A
A
Tanaka
N
N
Akutsu
N
N
Muro
M
M
Oshima
T
T
Imada
K
K
Sato
M
M
Katsube
Y
Y
D050539:3-Isopropylmalate Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000235:genetics*; D001412:Bacillus subtilis / Q000201:enzymology / Q000235:genetics; D003001:Cloning, Molecular; D003460:Crystallization; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D013824:Thermus / Q000201:enzymology / Q000235:genetics; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D000429:Alcohol Oxidoreductases; D050539:3-Isopropylmalate Dehydrogenase