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Purification and partial characterization of the Pyrococcus horikoshii methylmalonyl-CoA epimerase
1Department of Microbiology and Cell Science, University of Florida, Building 981, Room 1130, Gainesville, FL 32611, USA.
Applied Microbiology and Biotechnology
|October 31, 2003
Abstract:
Methylmalonyl-CoA epimerase (MCE) from the hyperthermophilic archaeon, Pyrococcus horikoshii, was expressed at high levels in Escherichia coli, purified, and partially characterized. The P. horikoshii MCE enzyme was a homodimer with an apparent molecular mass of 31,700 Da. The K(m) of the enzyme for methylmalonyl-CoA was 79 microM and the k(cat) was 240 s(-1). The P. horikoshii enzyme was extremely heat-stable and withstood boiling for 60 min without detectable loss in activity.