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.
PROSITE documentation PDOC00563Glycosyl hydrolases family 6 signatures
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC00563
The microbial degradation of cellulose and xylans requires several types of enzymes such as endoglucanases (EC 3.2.1.4), cellobiohydrolases (EC 3.2.1.91) (exoglucanases), or xylanases (EC 3.2.1.8) [1,2]. Fungi and bacteria produces a spectrum of cellulolytic enzymes (cellulases) and xylanases which, on the basis of sequence similarities, can be classified into families. One of these families is known as the cellulase family B [3] or as the glycosyl hydrolases family 6 [4,E1]. The enzymes which are currently known to belong to this family are listed below.
- Agaricus bisporus exoglucanase 3 (cel3).
- Cellulomonas fimi endoglucanase A (cenA).
- Cellulomonas fimi exoglucanase A (cbhA).
- Microspora bispora endoglucanase A (celA).
- Streptomyces halstedii endoglucanases A (celA1).
- Streptomyces strain KSM-9 endoglucanase 1 (casA).
- Thermomonospora fusca endoglucanase E-2 (celB).
- Trichoderma reesei exoglucanase II (CBH2).
One of the conserved regions in these enzymes contains a conserved aspartic acid residue which is potentially involved [5] in the catalytic mechanism; the aspartate is followed by a cysteine which is involved in a disulfide bond [6]. A second conserved region contains an aspartate which seems [5] to be the proton donor in the catalytic mechanism. We have used both regions as signature patterns.
Expert(s) to contact by email: Last update:May 2004 / Text revised.
-------------------------------------------------------------------------------
PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Beguin P. |
| Title | Molecular biology of cellulose degradation. | |
| Source | Annu. Rev. Microbiol. 44:219-248(1990). | |
| PubMed ID | 2252383 | |
| DOI | 10.1146/annurev.mi.44.100190.001251 |
| 2 | Authors | Gilkes N.R. Henrissat B. Kilburn D.G. Miller R.C. Jr. Warren R.A.J. |
| Title | Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families. | |
| Source | Microbiol. Rev. 55:303-315(1991). | |
| PubMed ID | 1886523 |
| 3 | Authors | Henrissat B. Claeyssens M. Tomme P. Lemesle L. Mornon J.-P. |
| Title | Cellulase families revealed by hydrophobic cluster analysis. | |
| Source | Gene 81:83-95(1989). | |
| PubMed ID | 2806912 |
| 4 | 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 |
| 5 | Authors | Rouvinen J. Bergfors T. Teeri T.T. Knowles J.K. Jones T.A. |
| Title | Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei. | |
| Source | Science 249:380-386(1990). | |
| PubMed ID | 2377893 |
| 6 | Authors | Gilkes N.R. Claeyssens M. Aebersold R. Henrissat B. Meinke A. Morrison H.D. Kilburn D.G. Warren R.A.J. Miller R.C. Jr. |
| Title | Structural and functional relationships in two families of beta-1,4-glycanases. | |
| Source | Eur. J. Biochem. 202:367-377(1991). | |
| PubMed ID | 1761039 |
| E1 | Title | https://www.uniprot.org/docs/glycosid |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.