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PROSITE documentation PDOC00531 |
It has been shown [1,2,E1] that the following glycosyl hydrolases can be, on the basis of sequence similarities, classified into a single family:
One of the conserved regions in these enzymes is centered on a conserved glutamic acid residue which has been shown [3], in Escherichia coli lacZ, to be the general acid/base catalyst in the active site of the enzyme. We have used this region as a signature pattern. As a second signature pattern we selected a highly conserved region located some sixty residues upstream from the active site glutamate.
Expert(s) to contact by email: Last update:April 2006 / Pattern revised.
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PROSITE methods (with tools and information) covered by this documentation:
1 | Authors | Henrissat B. |
Title | A classification of glycosyl hydrolases based on amino acid sequence similarities. | |
Source | Biochem. J. 280:309-316(1991). | |
PubMed ID | 1747104 |
2 | Authors | Schroeder C.J. Robert C. Lenzen G. McKay L.L. Mercenier A. |
Title | Analysis of the lacZ sequences from two Streptococcus thermophilus strains: comparison with the Escherichia coli and Lactobacillus bulgaricus beta-galactosidase sequences. | |
Source | J. Gen. Microbiol. 137:369-380(1991). | |
PubMed ID | 1901904 |
3 | Authors | Gebler J.C. Aebersold R. Withers S.G. |
Title | Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli. | |
Source | J. Biol. Chem. 267:11126-11130(1992). | |
PubMed ID | 1350782 |
E1 | Title | https://www.uniprot.org/docs/glycosid |