 |
|
| PROSITE documentation PDOC00910 |
Glycosyl hydrolases family 35 putative active site
Description:
β-galactosidases (EC 3.2.1.23) from mammals, fungi, plants and the bacteria
Xanthomonas manihotis are evolutionary related [1,2]. They belong to family 35
in the classification of glycosyl hydrolases [3,E1].
Mammalian β-galactosidase is a lysosomal enzyme (gene GLB1) which cleaves
the terminal galactose from gangliosides, glycoproteins, and
glycosaminoglycans and whose deficiency is the cause of the genetic disease
Gm(1) gangliosidosis (Morquio disease type B).
On of the best conserved regions in these enzymes contains a glutamic acid
residue which, on the basis of similarities with other families of glycosyl
hydrolases [4], probably acts as the proton donor in the catalytic mechanism.
We use this region as a signature pattern.
Expert(s) to contact by email:
Henrissat B.
Last update:
May 2004 / Text revised.
Technical section:
PROSITE method (with tools and information) covered by this documentation:
| GLYCOSYL_HYDROL_F35, PS01182; Glycosyl hydrolases family 35 putative active site (PATTERN) |
| Consensus pattern: |
G-G-P-[LIVM](2)-x(2)-Q-x-E-N-E-[FY]
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. |
|
|
|
| Matching PDB structures:
1TG7 1XC6 [ALL] |
References:
| 1 |
Authors | Taron C.H., Benner J.S., Hornstra L.J., Guthrie E.P. |
| Title | A novel beta-galactosidase gene isolated from the bacterium Xanthomonas manihotis exhibits strong homology to several eukaryotic beta-galactosidases. |
| Source | Glycobiology 5:603-610(1995). |
| PubMed ID | 8563148 |
| 2 |
Authors | Carey A.T., Holt K., Picard S., Wilde R., Tucker G.A., Bird C.R., Schuch W., Seymour G.B. |
| Title | Tomato exo-(1-->4)-beta-D-galactanase. Isolation, changes during ripening in normal and mutant tomato fruit, and characterization of a related cDNA clone. |
| Source | Plant Physiol. 108:1099-1107(1995). |
| PubMed ID | 7630937 |
| 3 |
Authors | Henrissat B., Bairoch A. |
| Title | New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. |
| Source | Biochem. J. 293:781-788(1993). |
| PubMed ID | 8352747 |
| 4 |
Authors | Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.-P., Davies G. |
| Title | Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. |
| Source | Proc. Natl. Acad. Sci. U.S.A. 92:7090-7094(1995). |
| PubMed ID | 7624375 |
Copyright:
PROSITE is copyright. It is produced 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. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to license@isb-sib.ch or
see: http://www.expasy.org/prosite/prosite_license.htm.
Miscellaneous:
View entry in original PROSITE document format
View entry in raw text format (no links)