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{PDOC00787}
{PS01027; GLYCOSYL_HYDROL_F39}
{BEGIN}
******************************************************
* Glycosyl hydrolases family 39 putative active site *
******************************************************
It has been shown [1,E1] that the following glycosyl hydrolases can be
classified into a single family on the basis of sequence similarities:
- Mammalian lysosomal alpha-L-iduronidase (EC 3.2.1.76).
- Caldocellum saccharolyticum and Thermoanaerobacter saccharolyticum beta-
xylosidase (EC 3.2.1.37) (gene xynB).
The best conserved regions in these enzymes is located in the N-terminal
section. It contains a glutamic acid residue which, on the basis of
similarities with other families of glycosyl hydrolases [2], probably acts as
the proton donor in the catalytic mechanism. We use this region as a signature
pattern.
-Consensus pattern: W-x-F-E-x-W-N-E-P-[DN]
[The second E may be the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Expert(s) to contact by email:
Henrissat B.; bernie@afmb.cnrs-mrs.fr
-Last update: May 2004 / Text revised.
[ 1] Henrissat B., Bairoch A.
"New families in the classification of glycosyl hydrolases based on
amino acid sequence similarities."
Biochem. J. 293:781-788(1993).
PubMed=8352747
[ 2] Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.-P., Davies G.
"Conserved catalytic machinery and the prediction of a common fold for
several families of glycosyl hydrolases."
Proc. Natl. Acad. Sci. U.S.A. 92:7090-7094(1995).
PubMed=7624375
[E1] http://www.expasy.org/cgi-bin/lists?glycosid.txt
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{END}
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