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. 1972 Oct;112(1):465–473. doi: 10.1128/jb.112.1.465-473.1972

Phosphotransacetylase from Clostridium acidiurici1

James R Robinson a, Richard D Sagers a
PMCID: PMC251433  PMID: 16559158

Abstract

The phosphotransacetylase from Clostridium acidiurici has two properties not observed for this enzyme in other bacteria: (i) it requires a divalent metal for activity, and (ii) it is not subject to uncoupling by arsenate. The enzyme has been obtained in highly purified form, with a specific activity 500-fold higher than crude extracts. Ferrous or manganous ions are required for maximal activity, with Mn2+ being 50 to 75% as effective as Fe2+. The acetyl group can be transferred from acetyl phosphate to coenzyme A in 20 mm arsenate without a net decrease in high-energy acyl linkages. Likewise, H32PO42− will exchange with acetyl-PO42− in the presence of arsenate without loss of acetyl phosphate. This suggests that the active site on the enzyme is capable of discriminating between phosphate and arsenate while permitting the reversible transfer of acyl groups between CoA and phosphate.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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