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. 1991 Dec;173(23):7719–7722. doi: 10.1128/jb.173.23.7719-7722.1991

Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm.

A I Derman 1, J Beckwith 1
PMCID: PMC212545  PMID: 1938970

Abstract

The cysteines of the Escherichia coli periplasmic enzyme alkaline phosphatase, which are involved in disulfide bonds in the native enzyme, were found to be fully reduced when the protein was retained in the cytoplasm. Under these circumstances the cysteines remained reduced for at least several minutes after the synthesis of the protein was completed. This contrasted with the normally exported protein, wherein disulfide bonds formed rapidly. Disulfide bond formation accompanied export and processing. The implications of these findings for the inactivity of the enzyme in the cytoplasm are discussed.

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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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