Jump to content

Talk:Chymotrypsin

Page contents not supported in other languages.
From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by 71.108.24.11 (talk) at 02:05, 28 November 2010 (Mechanism: new section). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

Template:Wikiproject MCB activating agent,active form, optimum pH of chymotrypsin

i may be wrong and misunderstand the author because i am not a native english speaker myself, however i believe he/she confused P and S. where the P site makes up the positions in the peptide to be hydrolysed and the S site the position in the active side of the protease interacting with the peptide to be cleave.

this can be looked up

ON THE SIZE OF THE ACTIVE SITE IN PROTEASES. I. PAPAIN BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS Vol. 27, No. 2, 1967 —Preceding unsigned comment added by Lohselose (talkcontribs) 17:35, 11 June 2010 (UTC)[reply]

Mechanism

The illustrated mechanism is wrong. The asp 102 does not deprotonate his 57. The hydrogen at that position in histidine isn't acidic to begin with. Asp 102 merely hydrogen bonds with his 57.