Re: O-GlcNAc

Ruth Hogue Angeletti (angelett@aecom.yu.edu)
Fri, 31 Jul 1998 08:28:09 -0400

Dear Leo,

There is only the single N-alpha-Fmoc group. However, they are
tri-O-acetyl derivatives.

Ruth

At 01:10 PM 7/30/98 -0400, Leo Benoiton wrote:
>Dear Ruth:
>
>I am very curious to know what is the formula of the Fmoc-derivative of
>N-acetylglucosamine? The amino group already is substituted with the acetyl
>group. Does the compound have the three hydroxy groups protected by Fmoc?
>
>Regards. Leo B.
>
>At 09:36 AM 98/7/30 -0400, you wrote:
>>Dear Rich,
>>
>>The Fmoc derivatives of GlcNAc and GalNAc are commercially available. Lisa
>>Mints in our group has used them to make peptides that performed well
>>during synthesis, cleavage, MALDI-MS analysis and HPLC. So, you should be
>>able to obtain peptides that you need.
>>
>>Best regards,
>>Ruth
>>
>>
>>
>>At 02:30 PM 7/29/98 -0800, Richard S. Johnson wrote:
>>>
>>> Does anyone know where one can obtain synthetic O-GlcNAc peptides?
If
>>> Gerald Hart is correct and O-GlcNAcylation is as common as
>>> phosphorylation it seems reasonable to wonder why no one seems to
come
>>> across this modification all that frequently. In the days prior to
>>> when mass spectrometers were in every other protein chem lab, one can
>>> understand why this modification was overlooked. Now that mass
>>> spectrometers are as common as vortexers, why don't people stumble
>>> across O-GlcNAc more often. A possible explanation, according to
>>> Gerald Hart is that O-GlcNAc is largely unstable to electrospray and
>>> maldi (including IR MALDI). Does anyone have any experience w/
>>> O-GlcNAc peptides or know how to obtain synthetic peptides?
>>>
>>> Regards, Rich Johnson (rjohnson@immunex.com)
>>>
>>>
>>>______________________________ Reply Separator
>>_________________________________
>>>Subject: Re: Posttranslational Modifications
>>>Author: Ken Mitchelhill <k.mitchelhill@medicine.unimelb.edu.au> at
Internet
>>>Date: 7/29/98 1:24 PM
>>>
>>>
>>>To: Ken Walsh
>>>
>>>Ken,
>>>
>>>In "the other Ken's" original post, he stated the doublet ran "about twice
>>>the distance between the phospho and non-phosho forms of either individual
>>>species" in isoelectric focussing.
>>>
>>>Gerald Hart presented his "dynamic glycosylation" data at Lorne this year
>>>and we have been looking out for it in some of the regulatory systems we
>>>are interested in. I am curious if you, or anyone else out there, knows
how
>>>GlcNacylation would be expected to affect the isoelectric mobility of a
>>>protein?
>>>
>>>regards....Ken Mitchelhill
>>>
>>>>Ken
>>>>
>>>>An interesting possibility for a PTM would be attachment of a single
>>>>hexosamine (+161). Gerald Hart has found that specific glycation (with
>>>>GlcNac I think) acts to limit phosphorylation.
>>>>
>>>>Ken
>>>>
>>>>Kenneth A. Walsh
>>>>E.W.Davie/ZymoGenetics Chair of Biochemistry
>>>>Box # 357350
>>>>University of Washington
>>>>Seattle WA 98195
>>>>
>>>>walsh@u.washington.edu
>>>>Phone 206-543-1768
>>>>FAX 206-685-9231
>>>>
>>>>On Mon, 27 Jul 1998, Kenneth Williams wrote:
>>>>
>>>>> One of our users is working with a kinase that is phosphorylated at a
>>>>> single site. In addition, however, the non-phosphorylated (and
>>>>> dephosphorylated) kinase migrates as a doublet on isoelectric
focussing -
>>>>> with the distance between the two (non-phosphorylated) species being
>>about
>>>>> twice the distance between the phospho and non-phosho forms of either
>>>>> individual species. My question is what are the most likely
>>>>> post-translational modifications that might give rise to the original
>>>>> doublet (assuming one species in not modified and that neiterh is
>>>>> phosphorylated).
>>>>>
>>>>> Thanks!
>>>>>
>>>>>
>>>>>
>>>>> Ken Williams, Ph.D.
>>>>> Director, HHMI Biopolymer/Keck Laboratory
>>>>> Professor (Adjunct) Research
>>>>> Molecular Biophysics and Biochemistry
>>>>>
>>>>>
>>>>> Visit the HHMI Biopolymer/Keck Laboratory Web Page at:
>>>>>
>>>>> http://info.med.yale.edu/wmkeck/
>>>>>
>>>>>
>>>
>>>
>>>********************************
>>>
>>>Ken I. Mitchelhill
>>>The John Holt Protein Structure Laboratory
>>>St. Vincent's Institute of Medical Research
>>>41 Victoria Parade
>>>Fitzroy 3065 Victoria
>>>AUSTRALIA
>>>
>>>Telephone: 61-3-9288 2480
>>>Facsimile: 61-3-9416 2676
>>>
>>>Email: k.mitchelhill@medicine.unimelb.edu.au
>>>
>>>Laboratory: http://www.medstv.unimelb.edu.au/WWWDOCS/SVIMRdocs/JHPSL.html
>>>ABRF: http://www.abrf.org
>>>
>>>***********************************
>>>
>>>
>>>
>>>
>>>
>>>
>>>
>>
>>
>N. Leo Benoiton
>Department of Biochemistry
>University of Ottawa
>Ottawa, Ontario, Canada K1H 8M5
>Tel: 613 562 5800, Ext. 8216
>Fax: 613 562 5440
>eMail: benoiton@uottawa.ca
>
>
>