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| PDOC00737 |
Glycosyl hydrolases family 25 active sites signature
Description:
It has been shown [1,2] that a number of cell-wall lytic enzymes (EC 3.2.1.17)
are evolutionary related and can be classified into a single family:
- Lysozymes (lysin) from Streptococcus pneumoniae bacteriophages of the Cp
family.
- Lysozyme (endolysin) from Lactococcus delbrueckii phage mv1.
- Autolytic lysozyme from Clostridium acetobutylicum.
- Lysozyme M1 from Streptomyces globisporus.
- N,O-diacetylmuramidase (lysozyme ch) from the fungus Chalaropsis.
Two residues, an aspartate and a glutamate, have been shown [3] to be
important for the catalytic activity of the Charalopsis enzyme. These residues
as well as some others in their vicinity are conserved in all proteins from
this family and can be used as a signature pattern.
Expert(s) to contact by email:
Henrissat B.
Last update:
December 2004 / Pattern and text revised.
Technical section:
PROSITE method (with tools and information) covered by this documentation:
| GLYCOSYL_HYDROL_F25, PS00953; Glycosyl hydrolases family 25 active sites signature (PATTERN) |
| Consensus pattern: |
D - [LIVM] - x(3) - [NQ] - [PGE] - x(9,15) - [GR] - x(4) - [LIVMFY](2) - K - x - [ST] - E - [GS] - x(2) - [FYL] - x - [DN]
D and E are active site residues |
| 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:
1H09 1JFX 1OBA 2IXU ... [ALL] |
References:
| 1 |
Authors | Croux C., Garcia J.L. |
| Title | Sequence of the lyc gene encoding the autolytic lysozyme of Clostridium acetobutylicum ATCC824: comparison with other lytic enzymes. |
| Source | Gene 104:25-31(1991). |
| PubMed ID | 1916274 |
| 2 |
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 |
| 3 |
Authors | Fouche P.B., Hash J.H. |
| Title | The N,O-diacetylmuramidase of Chalaropsis species. Identificaiton of aspartyl and glutamyl residues in the active site. |
| Source | J. Biol. Chem. 253:6787-6793(1978). |
| PubMed ID | 567645 |
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