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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1969 Nov;64(3):947–951. doi: 10.1073/pnas.64.3.947

ACTIVATION OF RABBIT LIVER FRUCTOSE DIPHOSPHATASE BY COENZYME A AND ACYL CARRIER PROTEIN*

K Nakashima 1,2,, S Pontremoli 1,2, B L Horecker 1,2
PMCID: PMC223326  PMID: 4313335

Abstract

The catalytic activity of rabbit liver fructose diphosphatase is enhanced more than fourfold by treatment with coenzyme A or acyl carrier protein. Other sulfhydryl compounds, such as glutathione or cysteine, are without effect. Activation is reversed by reduced glutathione or cysteine, indicating that the enzyme and activator are linked by disulfide bridges. The activated enzyme derivative can be formed by a disulfide exchange reaction at alkaline pH or by an oxidation reaction which proceeds at neutral pH. The latter process requires O2 and Cu++, and is inhibited by EDTA.

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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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