Literature DB >> 2658218

Enterokinase (enteropeptidase): comparative aspects.

A Light, H Janska.   

Abstract

The serine protease enterokinase is the physiological activator of trypsinogen and has a specificity for the sequence (Asp)4-Lys-Ile. The enzyme consists of two subunits linked by a disulfide bond. The heavy chain achors enterokinase in the intestinal brush border membrane and the light chain is the catalytic subunit, which has the same mechanism of action as trypsin and chymotrypsin. Many properties of enterokinase resemble blood-clotting enzymes, suggesting that enterokinase lies on the same phylogenetic branch as the blood-clotting proteins.

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Year:  1989        PMID： 2658218     DOI： 10.1016/0968-0004(89)90133-3

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN： 0968-0004            Impact factor:   13.807


  28 in total

1.  Enhancing the specificity of the enterokinase cleavage reaction to promote efficient cleavage of a fusion tag.

Authors:  S Hesam Shahravan; Xuanlu Qu; I-San Chan; Jumi A Shin
Journal:  Protein Expr Purif       Date:  2008-03-05       Impact factor: 1.650

2.  The SEA module: a new extracellular domain associated with O-glycosylation.

Authors:  P Bork; L Patthy
Journal:  Protein Sci       Date:  1995-07       Impact factor: 6.725

Review 3.  Regulation and function of mast cell proteases in inflammation.

Authors:  C Huang; A Sali; R L Stevens
Journal:  J Clin Immunol       Date:  1998-05       Impact factor: 8.317

4.  Identification of new tag sequences with differential and selective recognition properties for the anti-FLAG monoclonal antibodies M1, M2 and M5.

Authors:  J W Slootstra; D Kuperus; A Plückthun; R H Meloen
Journal:  Mol Divers       Date:  1997       Impact factor: 2.943

5.  Human enteropeptidase light chain: bioengineering of recombinants and kinetic investigations of structure and function.

Authors:  Eliot T Smith; David A Johnson
Journal:  Protein Sci       Date:  2013-03-26       Impact factor: 6.725

6.  Expansion of divergent SEA domains in cell surface proteins and nucleoporin 54.

Authors:  Jimin Pei; Nick V Grishin
Journal:  Protein Sci       Date:  2017-02-13       Impact factor: 6.725

7.  The UPEC pore-forming toxin α-hemolysin triggers proteolysis of host proteins to disrupt cell adhesion, inflammatory, and survival pathways.

Authors:  Bijaya K Dhakal; Matthew A Mulvey
Journal:  Cell Host Microbe       Date:  2012-01-19       Impact factor: 21.023

8.  Molecular characterization of two trypsinogens in the orange-spotted grouper, Epinephelus coioides, and their expression in tissues during early development.

Authors:  Chun-Hung Liu; Ya-Huei Chen; Ya-Li Shiu
Journal:  Fish Physiol Biochem       Date:  2012-07-17       Impact factor: 2.794

9.  The amino-terminal sequence of the catalytic subunit of bovine enterokinase.

Authors:  A Light; H Janska
Journal:  J Protein Chem       Date:  1991-10

10.  Mice expressing a mutant form of fibrinogen that cannot support fibrin formation exhibit compromised antimicrobial host defense.

Authors:  Joni M Prasad; Oleg V Gorkun; Harini Raghu; Sherry Thornton; Eric S Mullins; Joseph S Palumbo; Ya-Ping Ko; Magnus Höök; Tovo David; Shaun R Coughlin; Jay L Degen; Matthew J Flick
Journal:  Blood       Date:  2015-07-30       Impact factor: 22.113
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