Escherichia coli Signal Peptide Peptidase A Is a Serine-Lysine Protease with a Lysine Recruited to the Nonconserved Amino-Terminal Domain in the S49 Protease Family-Reference-Cited by-同舟云学术

Escherichia coli Signal Peptide Peptidase A Is a Serine-Lysine Protease with a Lysine Recruited to the Nonconserved Amino-Terminal Domain in the S49 Protease Family

Published:2008-05-14 Issue:24 Volume:47 Page:6361-6369
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Wang Peng¹,Shim Eunjung¹,Cravatt Benjamin¹,Jacobsen Richard¹,Schoeniger Joe¹,Kim Apollos C.¹,Paetzel Mark¹,Dalbey Ross E.¹

Affiliation:

1. Department of Chemistry, The Ohio State University, Columbus, Ohio 43210, Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada, The Skaggs Institute for Chemical Biology, Department of Cell Biology and Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, and Sandia National Laboratories, Livermore, California 94551-0969

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi800657p

Reference29 articles.

1. Signal Peptidases

2. Purification and characterization of leader (signal) peptidase from Escherichia coli.

3. Signal Peptide Digestion in Escherichia coli. Effect of Protease Inhibitors on Hydrolysis of the Cleaved Signal Peptide of the Major Outer-Membrane Lipoprotein

4. Protease IV, a cytoplasmic membrane protein of Escherichia coli, has signal peptide peptidase activity.

5. Purification and characterization of two novel proteolytic enzymes in membranes of Escherichia coli. Protease IV and protease V.

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