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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC00787
Glycosyl hydrolases family 39 putative active site


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PURL: https://purl.expasy.org/prosite/documentation/PDOC00787

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.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

GLYCOSYL_HYDROL_F39, PS01027; Glycosyl hydrolases family 39 active site  (PATTERN)


References

1AuthorsHenrissat B. Bairoch A.
TitleNew families in the classification of glycosyl hydrolases based on amino acid sequence similarities.
SourceBiochem. J. 293:781-788(1993).
PubMed ID8352747

2AuthorsHenrissat B. Callebaut I. Fabrega S. Lehn P. Mornon J.-P. Davies G.
TitleConserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.
SourceProc. Natl. Acad. Sci. U.S.A. 92:7090-7094(1995).
PubMed ID7624375

E1Titlehttps://www.uniprot.org/docs/glycosid



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