Science-advisor
REGISTER info/FAQ
Login
username
password
     
forgot password?
register here
 
Research articles
  search articles
  reviews guidelines
  reviews
  articles index
My Pages
my alerts
  my messages
  my reviews
  my favorites
 
 
Stat
Members: 3667
Articles: 2'599'751
Articles rated: 2609

17 February 2025
 
  » pubmed » pmid3838593

 Article overview



Redesigning trypsin: alteration of substrate specificity
C S Craik ; C Largman ; T Fletcher ; S Roczniak ; P J Barr ; R Fletterick ; W J Rutter ;
Date 19 Apr 1985
Journal Science, 228 (4697), 291-7
AbstractA general method for modifying eukaryotic genes by site-specific mutagenesis and subsequent expression in mammalian cells was developed to study the relation between structure and function of the proteolytic enzyme trypsin. Glycine residues at positions 216 and 226 in the binding cavity of trypsin were replaced by alanine residues, resulting in three trypsin mutants. Computer graphic analysis suggested that these substitutions would differentially affect arginine and lysine substrate binding of the enzyme. Although the mutant enzymes were reduced in catalytic rate, they showed enhanced substrate specificity relative to the native enzyme. This increased specificity was achieved by the unexpected differential effects on the catalytic activity toward arginine and lysine substrates. Mutants containing alanine at position 226 exhibited an altered conformation that may be converted to a trypsin-like structure upon binding of a substrate analog.
Source PubMed, pmid3838593
Services Forum | Review | Favorites   
 
Visitor rating: did you like this article? no 1   2   3   4   5   yes

No review found.
 Did you like this article?

This article or document is ...
important:
of broad interest:
readable:
new:
correct:
Global appreciation:

  Note: answers to reviews or questions about the article must be posted in the forum section.
Authors are not allowed to review their own article. They can use the forum section.






ScienXe.org
» my Online CV
» Free

home  |  contact  |  terms of use  |  sitemap
Copyright © 2005-2025 - Scimetrica