RE: trypsin/ogen catalytic triad

Kricker.Maja (kricker@NIEHS.NIH.GOV)
Mon, 08 May 1995 10:27:15 -0400

Hi, the protein Ethan Benatan and I are working on, acetylcholinesterase,
also has a calalytic triad. Although it has GLU instead of ASP, they
presumably work the same way. We made a protein and active site in BioMOO
that shows how things are presumed to work. Log into BioMOO using telnet or
your MUD client.Go to the Alanine room (go ala) then point your WWW browser
at http://bioinfo.weizmann.ac.il:8888. Choose authentication system, log in
using your username and password in BioMOO, choose The Viewer, and you are in
BioMOO. You will see a protein and an active site. Select each one to see
text and images. This is work in progress, so comments and corrections would
be greatly appreciated.

Or, if you want to be boring about the whole thing :-) you can just use the
following URL: http://enterprise.niehs.nih.gov/ACE.html. However, I will be
in the BioMOO Alanine room off and on or by appointment if anyone would like
to chat.

Maja Kricker PPS group: Alanine
http://enterprise.niehs.nih.gov/ maja on BioMOO
PPS protein: 1ACJ Acetylcholinesterase

_______________________________________________________________________________
I would like to understand the role of the
aspartic acid residue in the catalytic triad
(asp,his,ser) of trypsin/ogen. I understand what the
his and ser are doing during the peptide cleaving, but I
have not been able to figure out what the asp does? Can
someone explain this?
Gail I. Schuman
schuman@bnlstb.bio.bnl.gov

1TGN discussion in the works at:

http://bnlstb.bio.bnl.gov:8000/www_root/webdocs/pps/tryp
sin/trypsinogen.html