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- From: dexter@aries.scs.uiuc.edu (The Gecko)
- Subject: Re: Left-handed sugar
- References: <sfBC47y00WB7E3XZkG@andrew.cmu.edu> <72321@cup.portal.com> <72463@cup.portal.com> <1992Dec27.211004.24998@nntpd2.cxo.dec.com> <dexter.725570507@aries> <1992Dec28.231101.13255@nntpd2.cxo.dec.com> <dexter.725655833@aries> <1992Dec30.233312.27369@nntpd2.cxo.dec.com>
- Message-ID: <dexter.726081986@aries>
- Sender: usenet@news.cso.uiuc.edu (Net Noise owner)
- Organization: University of Illinois at Urbana
- Date: Sun, 3 Jan 1993 17:26:26 GMT
- Lines: 22
-
- winalski@adserv.enet.dec.com (Paul S. Winalski) writes:
-
- >According to my copy of Lehninger (regrettably quite old), the enzyme that
- >catalyzes the reaction fructose-1,6-diphosphate <-> DHAP + G-3-P (aldolase?)
- >is absolutely specific for dihydroxyactone phosphate, but will accept a
- >variety of aldehyde phosphates, or aldoses, in place of G-3-P. It will take
- >glyceraldehyde as well as its 3-phosphate, for example, to give
- >fructose-1-phosphate. This means that for aldolase at least, the configuration
- >about carbon 3 of the aldehyde substrate isn't a critical factor. It very
- >well might be that a D-configuration about this carbon is critical, however.
- >That's why I asked the question whether D/L specificity had been studied
- >for these enzymes (and the related ones of the Calvin cycle and pentose
- >phosphate shunt).
-
- The 3-carbon of glyceraldehyde does not have four different groups
- attached and so is not a contributor to chirality of the molecule. It is
- C-2 which is classified as D or L. Also, DHAP is not chiral, and so enzyme
- specificity here is not an issue of stereochemistry.
-
- Annette
-
-
-