PURIFICATION AND CHARACTERIZATION OF FORMYL-COENZYME-A TRANSFERASE FROM OXALOBACTER-FORMIGENES
PURIFICATION AND CHARACTERIZATION OF FORMYL-COENZYME-A TRANSFERASE FROM OXALOBACTER-FORMIGENES
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DOI：
10.1128/jb.172.7.3537-3540.1990
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发表时间：
1990-07-01
影响因子：
3.2
通讯作者：
ALLISON, MJ
中科院分区：
文献类型：
--
作者：
BAETZ, AL;ALLISON, MJ
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 in either oxalate or succinate. Apparent Km and Vmax values, respectively, were 3.0 mM and 29.6 .mu.mol/min per mg for formyl-CoA with an excess of succinate. The maximum specific activity was 2.15 .mu.mol of CoA transferred from formyl-CoA to oxalate per min per mg of protein.
