Literature DB >> 2819046

Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?

M M Dixon1, B W Matthews.   

Abstract

Refinement of the structure of gamma-chymotrypsin based on X-ray crystallographic data to 1.6-A resolution has confirmed the overall conformation of the molecule as reported previously [Cohen, G. H., Silverton, E. W., & Davies, D. R. (1981) J. Mol. Biol. 148, 449-479]. In addition, the new refinement suggests that gamma-chymotrypsin, which is operationally defined by its crystalline habit, may not be the free enzyme but rather a complex, possibly an acyl-enzyme adduct, with the tetrapeptide Pro-Gly-Ala-Tyr (or a close homologue). The crystallographic refinement provides a detailed geometrical description of the enzyme-substrate-solvent interactions that occur in the presumptive adduct.

Entities:  

Mesh：

Substances：

Year:  1989        PMID： 2819046     DOI： 10.1021/bi00443a038

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


  9 in total

1.  Observation of the light-triggered binding of pyrone to chymotrypsin by Laue x-ray crystallography.

Authors:  B L Stoddard; P Koenigs; N Porter; K Petratos; G A Petsko; D Ringe
Journal:  Proc Natl Acad Sci U S A       Date:  1991-07-01       Impact factor: 11.205

2.  Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates.

Authors:  Evette S Radisky; Justin M Lee; Chia-Jung Karen Lu; Daniel E Koshland
Journal:  Proc Natl Acad Sci U S A       Date:  2006-04-24       Impact factor: 11.205

3.  A preliminary neutron diffraction study of gamma-chymotrypsin.

Authors:  Walter R P Novak; Aaron G Moulin; Matthew P Blakeley; Ilme Schlichting; Gregory A Petsko; Dagmar Ringe
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2009-02-26

4.  Polarizable atomic multipole x-ray refinement: hydration geometry and application to macromolecules.

Authors:  Timothy D Fenn; Michael J Schnieders; Axel T Brunger; Vijay S Pande
Journal:  Biophys J       Date:  2010-06-16       Impact factor: 4.033

5.  Fractionation factors and activation energies for exchange of the low barrier hydrogen bonding proton in peptidyl trifluoromethyl ketone complexes of chymotrypsin.

Authors:  J Lin; W M Westler; W W Cleland; J L Markley; P A Frey
Journal:  Proc Natl Acad Sci U S A       Date:  1998-12-08       Impact factor: 11.205

6.  Inhibition of chymotrypsin by a complex of ortho-vanadate and benzohydroxamic acid: structure of the inert complex and its mechanistic interpretation.

Authors:  Aaron Moulin; Jason H Bell; R F Pratt; Dagmar Ringe
Journal:  Biochemistry       Date:  2007-05-01       Impact factor: 3.162

7.  Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).

Authors:  D Zhang; I Botos; F X Gomis-Rüth; R Doll; C Blood; F G Njoroge; J W Fox; W Bode; E F Meyer
Journal:  Proc Natl Acad Sci U S A       Date:  1994-08-30       Impact factor: 11.205

8.  Quantifying tetrahedral adduct formation and stabilization in the cysteine and the serine proteases.

Authors:  Jennifer A Cleary; William Doherty; Paul Evans; J Paul G Malthouse
Journal:  Biochim Biophys Acta       Date:  2015-07-11

9.  Correlation analysis of the side-chains conformational distribution in bound and unbound proteins.

Authors:  Tatsiana Kirys; Anatoly M Ruvinsky; Alexander V Tuzikov; Ilya A Vakser
Journal:  BMC Bioinformatics       Date:  2012-09-17       Impact factor: 3.169
  9 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.