Enhanced preference for π-bond containing substrates is correlated to Pro110 in the substrate-binding tunnel of Escherichia coli thioesterase I/protease I/lysophospholipase L1-Reference-Cited by-同舟云学术

Enhanced preference for π-bond containing substrates is correlated to Pro110 in the substrate-binding tunnel of Escherichia coli thioesterase I/protease I/lysophospholipase L1

Published:2007-08 Issue:8 Volume:1774 Page:959-967
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Lee Li-Chiun,Liaw Yen-Chywan,Lee Ya-Lin,Shaw Jei-Fu

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference24 articles.

1. Isolation and some properties of a proteolytic enzyme from Escherichia coli (protease I);Pacaud;Eur. J. Biochem.,1971

2. Studies on enzymes involved in the catabolism of phospholipids in Escherichia coli;Albright;J. Biol. Chem.,1973

3. Lysophospholipase of Escherichia coli;Doi;J. Biol. Chem.,1975

4. Protease I from Escherichia coli;Pacaud;Eur. J. Biochem.,1976

5. Lysophospholipase L1 from Escherichia coli K-12 overproducer;Karasawa;J. Biochem.,1991

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