From owner-btk-mca@hgmp.mrc.ac.uk Fri Jun 29 13:07:49 2001 Return-Path: Received: from localhost (localhost [127.0.0.1]) by mercury.hgmp.mrc.ac.uk (Postfix) with ESMTP id D383917B17 for ; Fri, 29 Jun 2001 13:07:46 +0100 (BST) Received: from localhost (localhost [127.0.0.1]) by mercury.hgmp.mrc.ac.uk (Postfix) with ESMTP id 3A9E117B13 for ; Fri, 29 Jun 2001 13:07:30 +0100 (BST) Received: from niobium.hgmp.mrc.ac.uk (niobium [193.62.192.41]) by mercury.hgmp.mrc.ac.uk (Postfix) with ESMTP id 3B11F17B14 for ; Fri, 29 Jun 2001 13:07:08 +0100 (BST) Received: (from news@localhost) by niobium.hgmp.mrc.ac.uk (8.9.3+Sun/8.8.8) id MAA24652 for btk-mca-list@hgmp.mrc.ac.uk; Fri, 29 Jun 2001 12:53:00 +0100 (BST) X-Authentication-Warning: niobium.hgmp.mrc.ac.uk: news set sender to using -f From: b.terkuile@chem.leidenuniv.nl ("Benno ter Kuile") X-Newsgroups: bionet.metabolic-reg Subject: Re: Enzymes!?! Date: 29 Jun 2001 12:52:59 +0100 Organization: R.U. Leiden Gorlaeus Lines: 19 Message-ID: References: <77754d4.0106281533.7930da7d@posting.google.com> Mime-Version: 1.0 Content-Type: text/plain; charset=US-ASCII Content-Transfer-Encoding: 7BIT X-Complaints-To: news@net.bio.net X-Received: from localhost (localhost [127.0.0.1]) by mercury.hgmp.mrc.ac.uk (Postfix) with ESMTP id 6B66417B0A for ; Fri, 29 Jun 2001 12:52:57 +0100 (BST) X-Received: from chem.leidenuniv.nl (chem.leidenuniv.nl [132.229.170.3]) by mercury.hgmp.mrc.ac.uk (Postfix) with SMTP id E63F017B17 for ; Fri, 29 Jun 2001 12:52:42 +0100 (BST) X-Received: from fwnc0162 (unverified [132.229.113.143]) by chem.leidenuniv.nl (EMWAC SMTPRS 0.83) with SMTP id ; Fri, 29 Jun 2001 13:51:20 +0200 X-To: btk-mca@hgmp.mrc.ac.uk X-Reply-To: b.terkuile@chem.leidenuniv.nl X-Priority: normal X-In-reply-to: <77754d4.0106281533.7930da7d@posting.google.com> X-Mailer: Pegasus Mail for Win32 (v3.12a) To: btk-mca@hgmp.mrc.ac.uk Sender: owner-btk-mca@hgmp.mrc.ac.uk Precedence: bulk I remember more than ten years ago listening in awe to Fred Opperdoes from Brussels giving a lecture about a joint project with Rik Wieringa, then in Heidelberg, on triosephosphateisomerase. They could show till the last hydrogen bridge how the intermediate forms were stabilized and the transition between the intermediates were facilitated. My conclusion would be that how enzymes work also very much depends on the enzyme studied and that you are likely to find different groups of mechanisms for different enzymes. Benno ter Kuile Benno ter Kuile Leiden Institute of Chemistry, Gorlaeus Laboratories. Leiden University;Einsteinweg 55 / P.O. Box 9502 2300RA, Leiden, The Netherlands. Phone: +31 71 5275272 TeleFax: +31 71 5274537 --- .