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PROSITE documentation PDOC00495 [for PROSITE entry PS00572] |
It has been shown [1,2,3,4] 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 [5], in the β-glucosidase from Agrobacterium, to be directly involved in glycosidic bond cleavage by acting as a nucleophile. We have used this region as a signature pattern. As a second signature pattern we selected a conserved region, found in the N-terminal extremity of these enzymes, this region also contains a glutamic acid residue.
Note:This pattern will pick up the last two domains of LPH; the first two domains, which are removed from the LPH precursor by proteolytic processing, have lost the active site glutamate and may therefore be inactive [4].
Consensus pattern:F-x-[FYWM]-[GSTA]-x-[GSTA]-x-[GSTA](2)-[FYNH]-[NQ]-x-E-x- [GSTA]
Sequences known to belong to this class detected by the pattern:ALL.
Other sequence(s) detected in Swiss-Prot:NONE.
Note:This pattern will pick up the last three domains of LPH.
Expert(s) to contact by email: Last update:November 1995 / Patterns and text 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 | Henrissat B. |
Title | Sequence homology between a beta-galactosidase and some beta-glucosidases. | |
Source | Protein Seq. Data Anal. 4:61-62(1991). | |
PubMed ID | 1924272 |
3 | Authors | Gonzalez-Candelas L. Ramon D. Polaina J. |
Source | Gene 95:31-38(1990). |
4 | Authors | El Hassouni M. Henrissat B. Chippaux M. Barras F. |
Source | J. Bacteriol. 174:765-777(1992). |
5 | Authors | Withers S.G. Warren R.A.J. Street I.P. Rupitz K. Kempton J.B. Aebersold R. |
Source | J. Am. Chem. Soc. 112:5887-5889(1990). |