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Literature DB >> 6153265

Thermodynamics and kinetics of the hydrolysis of the reactive-site peptide bond in pancreatic trypsin inhibitor (Kunitz) by Dermasterias imbricata trypsin 1.

D A Estell, K A Wilson, M Laskowski.

Abstract

Entities: Disease Species

Mesh：

Substances：

Year: 1980 PMID： 6153265 DOI： 10.1021/bi00542a020

Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162

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10 in total

Review 1. Biochemical and structural insights into mesotrypsin: an unusual human trypsin.

Authors: Moh'd A Salameh; Evette S Radisky
Journal: Int J Biochem Mol Biol Date: 2013-09-13

2. Mesotrypsin Has Evolved Four Unique Residues to Cleave Trypsin Inhibitors as Substrates.

Authors: Alexandre P Alloy; Olumide Kayode; Ruiying Wang; Alexandra Hockla; Alexei S Soares; Evette S Radisky
Journal: J Biol Chem Date: 2015-07-14 Impact factor: 5.157

3. An Acrobatic Substrate Metamorphosis Reveals a Requirement for Substrate Conformational Dynamics in Trypsin Proteolysis.

Authors: Olumide Kayode; Ruiying Wang; Devon F Pendlebury; Itay Cohen; Rachel D Henin; Alexandra Hockla; Alexei S Soares; Niv Papo; Thomas R Caulfield; Evette S Radisky
Journal: J Biol Chem Date: 2016-11-03 Impact factor: 5.157

4. Determinants of affinity and proteolytic stability in interactions of Kunitz family protease inhibitors with mesotrypsin.

Authors: Moh'd A Salameh; Alexei S Soares; Duraiswamy Navaneetham; Dipali Sinha; Peter N Walsh; Evette S Radisky
Journal: J Biol Chem Date: 2010-09-22 Impact factor: 5.157

5. The pH dependence of the equilibrium constant KHyd for the hydrolysis of the Lys15-Ala16 reactive-site peptide bond in bovine pancreatic trypsin inhibitor (aprotinin).

Authors: J Siekmann; H R Wenzel; E Matuszak; E von Goldammer; H Tschesche
Journal: J Protein Chem Date: 1988-10

Thermodynamics and kinetics of the hydrolysis of the reactive-site peptide bond in pancreatic trypsin inhibitor (Kunitz) by Dermasterias imbricata trypsin 1.

Review 1. Biochemical and structural insights into mesotrypsin: an unusual human trypsin.

2. Mesotrypsin Has Evolved Four Unique Residues to Cleave Trypsin Inhibitors as Substrates.

3. An Acrobatic Substrate Metamorphosis Reveals a Requirement for Substrate Conformational Dynamics in Trypsin Proteolysis.

4. Determinants of affinity and proteolytic stability in interactions of Kunitz family protease inhibitors with mesotrypsin.

5. The pH dependence of the equilibrium constant KHyd for the hydrolysis of the Lys15-Ala16 reactive-site peptide bond in bovine pancreatic trypsin inhibitor (aprotinin).

Review 6. Human mesotrypsin defies natural trypsin inhibitors: from passive resistance to active destruction.

7. Human mesotrypsin is a unique digestive protease specialized for the degradation of trypsin inhibitors.

8. Alteration of the disulfide-coupled folding pathway of BPTI by circular permutation.

9. Structure of a serine protease poised to resynthesize a peptide bond.

10. Effects of protease inhibitors and substrates on motility of mammalian spermatozoa.