Crystallization and preliminary X-ray analysis of an R-2-hydroxypropyl-coenzyme M dehydrogenase.
The R-2-hydroxypropyl-coenzyme M (2-mercaptoethanesulfonate) dehydrogenase is a key enzyme in the microbial conversion of propylene to the central metabolite acetoacetate. This enzyme is an interesting member of the NAD(P)H-dependent short-chain dehydrogenase/reductase (SDR) family of enzymes, being one of a pair of homologous dehydrogenases that act in concert in a single pathway to convert the R- and S-enantiomers of hydroxypropyl-coenzyme M to the achiral ketopropyl-coenzyme M product. Crystallization trials have revealed that the highest diffraction quality crystals (better than 2.0 A resolution) could be achieved when the reaction substrates were added to the enzyme in a stoichiometric excess prior to crystallization.
Department of Chemistry and Biochemistry, Montana State University, Bozeman 59717, USA.
Boguslaw
B
Nocek
Daniel D
DD
Clark
Scott A
SA
Ensign
John W
JW
Peters
D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry*; D011487:Protein Conformation; D020584:Xanthobacter / Q000201:enzymology*
D010088:Oxidoreductases