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. 1983 Oct 1;215(1):153–157. doi: 10.1042/bj2150153

A bifunctional enzyme complex in coenzyme A biosynthesis: purification of pantetheine phosphate adenylyltransferase and dephospho-CoA kinase.

D M Worrall, P K Tubbs
PMCID: PMC1152375  PMID: 6312972

Abstract

Pantetheine phosphate adenylyltransferase (EC 2.7.7.3) and dephospho-CoA kinase (EC 2.7.1.24) were purified to near homogeneity from pig liver. The purification steps included the use of Sepharose-linked triazine dyes and affinity elution by CoA. Both activities co-purified at every stage of the 18 000-fold purification. An Mr of 115 000 was obtained by gel filtration on Sephadex G-150, and the final preparation yielded one major band on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, with a subunit Mr of 57 000. It is concluded that pantetheine phosphate adenylyltransferase and dephospho-CoA kinase exist as a bifunctional dimeric protein, which could be designated CoA synthetase.

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Selected References

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