Glycoside hydrolase family 2 explained
| Symbol: | Glyco_hydro_2_N |
| Glycosyl hydrolases family 2, sugar binding domain |
| Pfam: | PF02837 |
| Pfam Clan: | CL0202 |
| Interpro: | IPR006104 |
| Prosite: | PDOC00531 |
| Scop: | 1bgl |
| Cazy: | GH2 |
| Symbol: | Glyco_hydro_2 |
| Glycosyl hydrolases family 2 |
| Pfam: | PF00703 |
| Interpro: | IPR006102 |
| Prosite: | PDOC00531 |
| Scop: | 1bgl |
| Cazy: | GH2 |
| Symbol: | Glyco_hydro_2_C |
| Glycosyl hydrolases family 2, TIM barrel domain |
| Pfam: | PF02836 |
| Pfam Clan: | CL0058 |
| Interpro: | IPR006103 |
| Prosite: | PDOC00531 |
| Scop: | 1bgl |
| Cazy: | GH2 |
In molecular biology, Glycoside hydrolase family 2 is a family of glycoside hydrolases, 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 2[8] comprises enzymes with several known activities: beta-galactosidase (EC 3.2.1.23); beta-mannosidase (EC 3.2.1.25); beta-glucuronidase (EC 3.2.1.31). These enzymes contain a conserved glutamic acid residue which has been shown,[9] in Escherichia coli lacZ, to be the general acid/base catalyst in the active site of the enzyme.
The catalytic domain of Beta-galactosidases have a TIM barrel core surrounded several other largely beta domains.[10] The sugar binding domain of these proteins has a jelly-roll fold.[10] These enzymes also include an immunoglobulin-like beta-sandwich domain.[10]
External links
Notes and References
- Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G . 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 . July 1995 . 7624375 . 41477 . 10.1073/pnas.92.15.7090 . 1995PNAS...92.7090H . free .
- Davies G, Henrissat B . Structures and mechanisms of glycosyl hydrolases . Structure . 3 . 9 . 853–9 . September 1995 . 8535779 . 10.1016/S0969-2126(01)00220-9 . free .
- Henrissat B, Bairoch A . Updating the sequence-based classification of glycosyl hydrolases . The Biochemical Journal . 316 . Pt 2 . 695–6 . June 1996 . 8687420 . 1217404 . 10.1042/bj3160695.
- Web site: Home. CAZy.org. en. 2018-03-06.
- Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, Henrissat B . The carbohydrate-active enzymes database (CAZy) in 2013 . Nucleic Acids Research . 42 . Database issue . D490-5 . January 2014 . 24270786 . 3965031 . 10.1093/nar/gkt1178 .
- Web site: Glycoside Hydrolase Family 2. CAZypedia.org. en. 2018-03-06.
- Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes . Glycobiology . 28 . 1 . 3–8 . December 2018 . 29040563 . 10.1093/glycob/cwx089 . CAZypedia Consortium . free .
- Web site: Glycoside Hydrolase Family 2 (GH_2) . Withers S . CAZypedia - carbohydrate active enzymes . 2010-10-10 .
- Gebler JC, Aebersold R, Withers SG . Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli . The Journal of Biological Chemistry . 267 . 16 . 11126–30 . June 1992 . 10.1016/S0021-9258(19)49884-0 . 1350782 . free .
- Jacobson RH, Zhang XJ, DuBose RF, Matthews BW . Three-dimensional structure of beta-galactosidase from E. coli . Nature . 369 . 6483 . 761–6 . June 1994 . 8008071 . 10.1038/369761a0 . 1994Natur.369..761J . 4241867 .
