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. 1990 Jul;172(7):3537-40.
doi: 10.1128/jb.172.7.3537-3540.1990.

Purification and characterization of formyl-coenzyme A transferase from Oxalobacter formigenes

A L Baetz  1 , M J Allison
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Purification and characterization of formyl-coenzyme A transferase from Oxalobacter formigenes

A L Baetz et al. J Bacteriol. 1990 Jul.

Abstract

Formyl-coenzyme A (formyl-CoA) transferase was purified from Oxalobacter formigenes by high-pressure liquid chromatography with hydrophobic interaction chromatography and by DEAE anion-exchange chromatography. The enzyme was a single entity on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel permeation chromatography (Mr, 44,000). It had an isoelectric point of 4.7. The enzyme catalyzed the transfer of CoA from formyl-CoA to either oxalate or succinate. Apparent Km and Vmax values, respectively, were 3.0 mM and 29.6 mumols/min per mg for formyl-CoA with an excess of succinate. The maximum specific activity was 2.15 mumols of CoA transferred from formyl-CoA to oxalate per min per mg of protein.

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