Jump to content

  • Log in with Facebook Log in with Twitter Log in with Windows Live Log In with Google      Sign In   
  • Create Account

Submit your paper to J Biol Methods today!
- - - - -

How do mutations distal to the active site effect activity?

  • Please log in to reply
1 reply to this topic

#1 cwilsonbran



  • Active Members
  • Pip
  • 5 posts

Posted 24 August 2011 - 06:23 AM


I want to study how mutations distal to the active site effect the activity of the enzyme. I'm looking for a smaller protein 15KD to 35KD (I'll be using NMR and hi-throughput crystallization) which sees an increase in activity along a evolutionary path say E.coli -> Yeast, Yeast -> mammal. something within this span. I want a protein that depsite the increase in activity shows little change in the active site.

I know of a couple but all are too large.

any suggestions.

Thank you

#2 prodes



  • Active Members
  • Pip
  • 25 posts

Posted 25 August 2011 - 11:51 AM

1) One option is aaRS - aminoacyl-tRNA synthetases catalytic domains not very big and highly conserved. Some structures exist, some enzymes are bigger than others option to focus on editing or catalytic domains.
2) Another classic enzyme is from the glucose metabolism e.g. Glyceraldehyde-3-phosphate dehydrogenase A. There are crystal structures, on the upper limit of size for the NMR.

I think that is a very interesting subject. Highly relevant is almost any directed evolution enzyme for improved thermostability or processivity (often mutations are in the second or outer shell from the catalytic site).

Home - About - Terms of Service - Privacy - Contact Us

©1999-2013 Protocol Online, All rights reserved.