| Cellulase (glycosyl hydrolase family 5) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Cellulase | ||||||||
| Pfam | PF00150 | ||||||||
| Pfam clan | CL0058 | ||||||||
| InterPro | IPR001547 | ||||||||
| PROSITE | PDOC00565 | ||||||||
| SCOP2 | 2exo / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 117 | ||||||||
| OPM protein | 2osx | ||||||||
| CAZy | GH5 | ||||||||
| Membranome | 1365 | ||||||||
| |||||||||
In molecular biology, glycoside hydrolase family 5 is a family of glycoside hydrolases EC 3.2.1., which are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. [1] [2] [3] This classification is available on the CAZy web site, [4] [5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes. [6] [7]
Glycoside hydrolase family 5 CAZY GH_5 comprises enzymes with several known activities including endoglucanase ( EC 3.2.1.4); beta-mannanase ( EC 3.2.1.78); exo-1,3-glucanase ( EC 3.2.1.58); endo-1,6-glucanase ( EC 3.2.1.75); xylanase ( EC 3.2.1.8); endoglycoceramidase ( EC 3.2.1.123); xanthanase. [8]
The microbial degradation of cellulose and xylans requires several types of enzymes. 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 A [9] or as the glycosyl hydrolases family 5. [10] One of the conserved regions in this family contains a conserved glutamic acid residue which is potentially involved [11] in the catalytic mechanism.
In a recent study using Molecular Dynamics simulations, a considerable correlation between thermal stability and structural rigidity of members of family 5 with solved structures has been proved. [12]
External links
References
- ^ Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G (July 1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proceedings of the National Academy of Sciences of the United States of America. 92 (15): 7090–4. Bibcode: 1995PNAS...92.7090H. doi: 10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375.
- ^ Davies G, Henrissat B (September 1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–9. doi: 10.1016/S0969-2126(01)00220-9. PMID 8535779.
- ^ Henrissat B, Bairoch A (June 1996). "Updating the sequence-based classification of glycosyl hydrolases". The Biochemical Journal. 316 (Pt 2): 695–6. doi: 10.1042/bj3160695. PMC 1217404. PMID 8687420.
- ^ "Home". CAZy.org. Retrieved 2018-03-06.
- ^ Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, Henrissat B (January 2014). "The carbohydrate-active enzymes database (CAZy) in 2013". Nucleic Acids Research. 42 (Database issue): D490-5. doi: 10.1093/nar/gkt1178. PMC 3965031. PMID 24270786.
- ^ "Glycoside Hydrolase Family 5". CAZypedia.org. Retrieved 2018-03-06.
- ^ CAZypedia Consortium (December 2018). "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes" (PDF). Glycobiology. 28 (1): 3–8. doi: 10.1093/glycob/cwx089. hdl: 21.11116/0000-0003-B7EB-6. PMID 29040563.
- ^ Ostrowski, Matthew P.; La Rosa, Sabina Leanti; Kunath, Benoit J.; Robertson, Andrew; Pereira, Gabriel; Hagen, Live H.; Varghese, Neha J.; Qiu, Ling; Yao, Tianming; Flint, Gabrielle; Li, James; McDonald, Sean P.; Buttner, Duna; Pudlo, Nicholas A.; Schnizlein, Matthew K.; Young, Vincent B.; Brumer, Harry; Schmidt, Thomas M.; Terrapon, Nicolas; Lombard, Vincent; Henrissat, Bernard; Hamaker, Bruce; Eloe-Fadrosh, Emiley A.; Tripathi, Ashootosh; Pope, Phillip B.; Martens, Eric C. (April 2022). "Mechanistic insights into consumption of the food additive xanthan gum by the human gut microbiota". Nature Microbiology. 7 (4): 556–569. doi: 10.1038/s41564-022-01093-0. hdl: 11250/3003739. PMID 35365790. S2CID 247866305.
- ^ Henrissat B, Claeyssens M, Tomme P, Lemesle L, Mornon JP (September 1989). "Cellulase families revealed by hydrophobic cluster analysis". Gene. 81 (1): 83–95. doi: 10.1016/0378-1119(89)90339-9. PMID 2806912.
- ^ Henrissat B (December 1991). "A classification of glycosyl hydrolases based on amino acid sequence similarities". The Biochemical Journal. 280 (2): 309–16. doi: 10.1042/bj2800309. PMC 1130547. PMID 1747104.
- ^ Py B, Bortoli-German I, Haiech J, Chippaux M, Barras F (February 1991). "Cellulase EGZ of Erwinia chrysanthemi: structural organization and importance of His98 and Glu133 residues for catalysis". Protein Engineering. 4 (3): 325–33. doi: 10.1093/protein/4.3.325. PMID 1677466.
- ^ Badieyan S, Bevan DR, Zhang C (January 2012). "Study and design of stability in GH5 cellulases". Biotechnology and Bioengineering. 109 (1): 31–44. doi: 10.1002/bit.23280. PMID 21809329. S2CID 29281420.
| Cellulase (glycosyl hydrolase family 5) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Cellulase | ||||||||
| Pfam | PF00150 | ||||||||
| Pfam clan | CL0058 | ||||||||
| InterPro | IPR001547 | ||||||||
| PROSITE | PDOC00565 | ||||||||
| SCOP2 | 2exo / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 117 | ||||||||
| OPM protein | 2osx | ||||||||
| CAZy | GH5 | ||||||||
| Membranome | 1365 | ||||||||
| |||||||||
In molecular biology, glycoside hydrolase family 5 is a family of glycoside hydrolases EC 3.2.1., which are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. [1] [2] [3] This classification is available on the CAZy web site, [4] [5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes. [6] [7]
Glycoside hydrolase family 5 CAZY GH_5 comprises enzymes with several known activities including endoglucanase ( EC 3.2.1.4); beta-mannanase ( EC 3.2.1.78); exo-1,3-glucanase ( EC 3.2.1.58); endo-1,6-glucanase ( EC 3.2.1.75); xylanase ( EC 3.2.1.8); endoglycoceramidase ( EC 3.2.1.123); xanthanase. [8]
The microbial degradation of cellulose and xylans requires several types of enzymes. 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 A [9] or as the glycosyl hydrolases family 5. [10] One of the conserved regions in this family contains a conserved glutamic acid residue which is potentially involved [11] in the catalytic mechanism.
In a recent study using Molecular Dynamics simulations, a considerable correlation between thermal stability and structural rigidity of members of family 5 with solved structures has been proved. [12]
External links
References
- ^ Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G (July 1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proceedings of the National Academy of Sciences of the United States of America. 92 (15): 7090–4. Bibcode: 1995PNAS...92.7090H. doi: 10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375.
- ^ Davies G, Henrissat B (September 1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–9. doi: 10.1016/S0969-2126(01)00220-9. PMID 8535779.
- ^ Henrissat B, Bairoch A (June 1996). "Updating the sequence-based classification of glycosyl hydrolases". The Biochemical Journal. 316 (Pt 2): 695–6. doi: 10.1042/bj3160695. PMC 1217404. PMID 8687420.
- ^ "Home". CAZy.org. Retrieved 2018-03-06.
- ^ Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, Henrissat B (January 2014). "The carbohydrate-active enzymes database (CAZy) in 2013". Nucleic Acids Research. 42 (Database issue): D490-5. doi: 10.1093/nar/gkt1178. PMC 3965031. PMID 24270786.
- ^ "Glycoside Hydrolase Family 5". CAZypedia.org. Retrieved 2018-03-06.
- ^ CAZypedia Consortium (December 2018). "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes" (PDF). Glycobiology. 28 (1): 3–8. doi: 10.1093/glycob/cwx089. hdl: 21.11116/0000-0003-B7EB-6. PMID 29040563.
- ^ Ostrowski, Matthew P.; La Rosa, Sabina Leanti; Kunath, Benoit J.; Robertson, Andrew; Pereira, Gabriel; Hagen, Live H.; Varghese, Neha J.; Qiu, Ling; Yao, Tianming; Flint, Gabrielle; Li, James; McDonald, Sean P.; Buttner, Duna; Pudlo, Nicholas A.; Schnizlein, Matthew K.; Young, Vincent B.; Brumer, Harry; Schmidt, Thomas M.; Terrapon, Nicolas; Lombard, Vincent; Henrissat, Bernard; Hamaker, Bruce; Eloe-Fadrosh, Emiley A.; Tripathi, Ashootosh; Pope, Phillip B.; Martens, Eric C. (April 2022). "Mechanistic insights into consumption of the food additive xanthan gum by the human gut microbiota". Nature Microbiology. 7 (4): 556–569. doi: 10.1038/s41564-022-01093-0. hdl: 11250/3003739. PMID 35365790. S2CID 247866305.
- ^ Henrissat B, Claeyssens M, Tomme P, Lemesle L, Mornon JP (September 1989). "Cellulase families revealed by hydrophobic cluster analysis". Gene. 81 (1): 83–95. doi: 10.1016/0378-1119(89)90339-9. PMID 2806912.
- ^ Henrissat B (December 1991). "A classification of glycosyl hydrolases based on amino acid sequence similarities". The Biochemical Journal. 280 (2): 309–16. doi: 10.1042/bj2800309. PMC 1130547. PMID 1747104.
- ^ Py B, Bortoli-German I, Haiech J, Chippaux M, Barras F (February 1991). "Cellulase EGZ of Erwinia chrysanthemi: structural organization and importance of His98 and Glu133 residues for catalysis". Protein Engineering. 4 (3): 325–33. doi: 10.1093/protein/4.3.325. PMID 1677466.
- ^ Badieyan S, Bevan DR, Zhang C (January 2012). "Study and design of stability in GH5 cellulases". Biotechnology and Bioengineering. 109 (1): 31–44. doi: 10.1002/bit.23280. PMID 21809329. S2CID 29281420.