| Literature DB >> 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.Entities:
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Year: 1991 PMID: 1938970 PMCID: PMC212545 DOI: 10.1128/jb.173.23.7719-7722.1991
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490