Literature DB >> 33696

Mechanism of association of a specific aldehyde "transition-state analogue" to the active site of alpha-chymotrypsin.

W P Kennedy, R M Schultz.   

Abstract

Entities:  

Mesh：

Substances：

Year:  1979        PMID： 33696     DOI： 10.1021/bi00569a019

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


× No keyword cloud information.
  4 in total

1.  Slow tight-binding inhibition of prolyl endopeptidase by benzyloxycarbonyl-prolyl-prolinal.

Authors:  A V Bakker; S Jung; R W Spencer; F J Vinick; W S Faraci
Journal:  Biochem J       Date:  1990-10-15       Impact factor: 3.857

2.  Tumor cell proteinase visualization and quantification using a fluorescent transition-state analog probe.

Authors:  K A Kozlowski; F H Wezeman; R M Schultz
Journal:  Proc Natl Acad Sci U S A       Date:  1984-02       Impact factor: 11.205

3.  Preparations of psi-peptide bond and peptide-aldehyde inhibitors of atrial granule serine proteinase, a candidate processing enzyme of pro-atrial natriuretic factor.

Authors:  A Damodaran; R B Harris
Journal:  J Protein Chem       Date:  1995-08

4.  Hemiacetal stabilization in a chymotrypsin inhibitor complex and the reactivity of the hydroxyl group of the catalytic serine residue of chymotrypsin.

Authors:  Jennifer A Cleary; William Doherty; Paul Evans; J Paul G Malthouse
Journal:  Biochim Biophys Acta       Date:  2014-03-21
  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.