Purification and Characterization of methylmalonyl-CoA Epimerase From Propionibacterium Shermanii

Biochem J. 1981 Aug 1;197(2):413-9. doi: 10.1042/bj1970413.

Abstract

Methylmalonyl-CoA epimerase, which specifically interconverts the (2R)- and (2S)- epimers of methylmalonyl-CoA, was purified 95-fold from Propionibacterium shermanii by a new method that affords apparently homogeneous enzyme, in 80-100mg quantities, in yields representing about 40% of the activity in cell-free extracts. The specific activity of the purified enzyme, 10.1 mukat/mg, is much greater than previously reported. Native methylmalonyl-CoA epimerase has Mr about 33000, and apparently consists of two identical subunits. The purified enzyme is stable indefinitely when stored at -20 degrees C and pH 8.5, but contrary to previous reports it is not unusually acid-stable. The activity of methylmalonyl-CoA epimerase is increased by Co2+, and to a smaller extent by Ni2+, Mn2+ and Zn2+.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Cations, Divalent / pharmacology
  • Chemical Phenomena
  • Chemistry
  • Chromatography, Gel
  • Electrophoresis, Polyacrylamide Gel
  • Isomerases* / isolation & purification
  • Metals / analysis
  • Propionibacterium / enzymology*
  • Racemases and Epimerases* / antagonists & inhibitors
  • Racemases and Epimerases* / isolation & purification

Substances

  • Amino Acids
  • Cations, Divalent
  • Metals
  • Isomerases
  • Racemases and Epimerases
  • methylmalonyl-coenzyme A racemase