Crystallization and preliminary X-ray analysis of a NADPH 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.
NADPH 2-ketopropyl-coenzyme M (2-mercaptoethanesulfonate) oxidoreductase/carboxylase is the terminal enzyme in a metabolic pathway that results in the conversion of propylene to the central metabolite acetoacetate. This enzyme is an FAD-containing enzyme that is a member of the NADPH:disulfide oxidoreductase family of enzymes and catalyzes the cleavage and carboxylation of 2-ketopropyl-coenzyme M to form acetoacetate and coenzyme M. Crystallization trials have revealed that the highest diffraction quality crystals (better that 2.0 A resolution) could be achieved when the substrate or product of the reaction was added to the enzyme in a stoichiometric excess.
Department of Chemistry and Biochemistry, Utah State University, Logan, UT 84322-0300, USA.
S B
SB
Jang
M S
MS
Jeong
D D
DD
Clark
S A
SA
Ensign
J W
JW
Peters
D003460:Crystallization; D018360:Crystallography, X-Ray; D007658:Ketone Oxidoreductases / Q000737:chemistry*; D015080:Mesna / Q000737:chemistry; D009249:NADP / Q000737:chemistry; D010088:Oxidoreductases / Q000737:chemistry; D011487:Protein Conformation; D020584:Xanthobacter / Q000201:enzymology*
D009249:NADP; D010088:Oxidoreductases; D007658:Ketone Oxidoreductases; C425603:2-KPCC; D015080:Mesna