Characterization of a soluble, catalytically active form of Escherichia coli leader peptidase: requirement of detergent or phospholipid for optimal activity-Reference-Cited by-同舟云学术

Characterization of a soluble, catalytically active form of Escherichia coli leader peptidase: requirement of detergent or phospholipid for optimal activity

Published:1995-03-28 Issue:12 Volume:34 Page:3935-3941
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Tschantz William,Paetzel Mark,Cao Guoqing,Suciu Dominic,Inouye Masayori,Dalbey Ross E.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00012a010

Reference36 articles.

1. Detergent removal during membrane reconstitution

2. Mapping of catalytically important domains in Escherichia coli leader peptidase.

3. Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad

4. Phase separation of integral membrane proteins in Triton X-114 solution.

5. Determination ofKm andkcat for Signal Peptidase I Using a Full Length Secretory Precursor, pro-OmpA-nuclease A

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