Purification and characterization of formyl-coenzyme A transferase from Oxalobacter formigenes.
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Baetz AL, Allison MJ
Purification and characterization of formyl-coenzyme A transferase from Oxalobacter formigenes.
J Bacteriol. 1990 Jul;172(7):3537-40.
- PubMed ID
- 2361939 [ View in PubMed]
- 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.