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

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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Derman AI,Beckwith J

doi

10.1128/jb.173.23.7719-7722.1991

subject

Has Abstract

pub_date

1991-12-01 00:00:00

pages

7719-22

issue

23

eissn

0021-9193

issn

1098-5530

journal_volume

173

pub_type

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