{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 is the putative 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: November 1997 / Text revised. [ 1] Henrissat B., Bairoch A. Biochem. J. 293:781-788(1993). [ 2] Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.-P., Davies G. Proc. Natl. Acad. Sci. U.S.A. 92:7090-7094(1995). [E1] http://www.expasy.ch/cgi-bin/lists?glycosid.txt +----------------------------------------------------------------------------+ | This PROSITE entry is copyright by the Swiss Institute of Bioinformatics | | (SIB). There are no restrictions on its use by non-profit institutions as | | long as its content is in no way modified and this statement is not | | removed. Usage by and for commercial entities requires a license agreement | | (See http://www.isb-sib.ch/announce/ or email to license@isb-sib.ch). | +----------------------------------------------------------------------------+ {END}