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| PROSITE documentation PDOC00787 |
Glycosyl hydrolases family 39 putative active site
Description:
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 α-L-iduronidase (EC 3.2.1.76).
- Caldocellum saccharolyticum and Thermoanaerobacter saccharolyticum β-
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.
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_F39, PS01027; Glycosyl hydrolases family 39 active site (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. |
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| Matching PDB structures:
1PX8 1UHV 1W91 1Y24 ... [ALL] |
References:
| 1 |
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 |
| 2 |
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 |
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