Literature DB >> 18259688

Serine peptidases: classification, structure and function.

M J Page1, E Di Cera.   

Abstract

Serine peptidases play key roles in human health and disease and their biochemical properties shaped the molecular evolution of these processes. Of known proteolytic enzymes, the serine peptidase family is the major cornerstone of the vertebrate degradome. We describe the known diversity of serine peptidases with respect to structure and function. Particular emphasis is placed on the S1 peptidase family, the trypsins, which underwent the most predominant genetic expansion yielding the enzymes responsible for vital processes in man such as digestion, blood coagulation, fibrinolysis, development, fertilization, apoptosis and immunity.

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Year:  2008        PMID: 18259688     DOI: 10.1007/s00018-008-7565-9

Source DB:  PubMed          Journal:  Cell Mol Life Sci        ISSN: 1420-682X            Impact factor:   9.261


  136 in total

Review 1.  Conformational selection in trypsin-like proteases.

Authors:  Nicola Pozzi; Austin D Vogt; David W Gohara; Enrico Di Cera
Journal:  Curr Opin Struct Biol       Date:  2012-06-03       Impact factor: 6.809

2.  WEDGE: an anticoagulant thrombin mutant produced by autoactivation.

Authors:  D C Wood; L A Pelc; N Pozzi; M Wallisch; N G Verbout; E I Tucker; A Gruber; E Di Cera
Journal:  J Thromb Haemost       Date:  2014-11-29       Impact factor: 5.824

3.  Exposure of R169 controls protein C activation and autoactivation.

Authors:  Nicola Pozzi; Sergio Barranco-Medina; Zhiwei Chen; Enrico Di Cera
Journal:  Blood       Date:  2012-04-24       Impact factor: 22.113

4.  Molecular basis for the resistance of an insect chymotrypsin to a potato type II proteinase inhibitor.

Authors:  K M Dunse; Q Kaas; R F Guarino; P A Barton; D J Craik; M A Anderson
Journal:  Proc Natl Acad Sci U S A       Date:  2010-08-09       Impact factor: 11.205

5.  Crystal structure of thrombin bound to the uncleaved extracellular fragment of PAR1.

Authors:  Prafull S Gandhi; Zhiwei Chen; Enrico Di Cera
Journal:  J Biol Chem       Date:  2010-03-17       Impact factor: 5.157

6.  Mechanisms and specificity of factor XIa and trypsin inhibition by protease nexin 2 and basic pancreatic trypsin inhibitor.

Authors:  Duraiswamy Navaneetham; Dipali Sinha; Peter N Walsh
Journal:  J Biochem       Date:  2010-07-20       Impact factor: 3.387

7.  Kinetic dissection of the pre-existing conformational equilibrium in the trypsin fold.

Authors:  Austin D Vogt; Pradipta Chakraborty; Enrico Di Cera
Journal:  J Biol Chem       Date:  2015-07-27       Impact factor: 5.157

8.  Why Ser and not Thr brokers catalysis in the trypsin fold.

Authors:  Leslie A Pelc; Zhiwei Chen; David W Gohara; Austin D Vogt; Nicola Pozzi; Enrico Di Cera
Journal:  Biochemistry       Date:  2015-02-11       Impact factor: 3.162

9.  Na+ binding to meizothrombin desF1.

Authors:  M E Papaconstantinou; P S Gandhi; Z Chen; A Bah; E Di Cera
Journal:  Cell Mol Life Sci       Date:  2008-11       Impact factor: 9.261

10.  Amide Rotation Hindrance Predicts Proteolytic Resistance of Cystine-Knot Peptides.

Authors:  Yanzi Zhou; Daiqian Xie; Yingkai Zhang
Journal:  J Phys Chem Lett       Date:  2016-03-11       Impact factor: 6.475

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