PROSITE documentation 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)


References

1AuthorsCroux C., Garcia J.L.
TitleSequence of the lyc gene encoding the autolytic lysozyme of Clostridium acetobutylicum ATCC824: comparison with other lytic enzymes.
SourceGene 104:25-31(1991).
PubMed ID1916274

2AuthorsHenrissat B.
TitleA classification of glycosyl hydrolases based on amino acid sequence similarities.
SourceBiochem. J. 280:309-316(1991).
PubMed ID1747104

3AuthorsFouche P.B., Hash J.H.
TitleThe N,O-diacetylmuramidase of Chalaropsis species. Identificaiton of aspartyl and glutamyl residues in the active site.
SourceJ. Biol. Chem. 253:6787-6793(1978).
PubMed ID567645



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