Glycoside hydrolase family 2
| Glycosyl hydrolases family 2, sugar binding domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 e. coli (lacz) beta-galactosidase-trapped 2-deoxy-galactosyl enzyme intermediate | |||||||||
| Identifiers | |||||||||
| Symbol | Glyco_hydro_2_N | ||||||||
| Pfam | PF02837 | ||||||||
| Pfam clan | CL0202 | ||||||||
| InterPro | IPR006104 | ||||||||
| PROSITE | PDOC00531 | ||||||||
| SCOP2 | 1bgl / SCOPe / SUPFAM | ||||||||
| CAZy | GH2 | ||||||||
| |||||||||
| Glycosyl hydrolases family 2 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
e. coli (lacz) beta-galactosidase-trapped 2-deoxy-galactosyl enzyme intermediate | |||||||||
| Identifiers | |||||||||
| Symbol | Glyco_hydro_2 | ||||||||
| Pfam | PF00703 | ||||||||
| InterPro | IPR006102 | ||||||||
| PROSITE | PDOC00531 | ||||||||
| SCOP2 | 1bgl / SCOPe / SUPFAM | ||||||||
| CAZy | GH2 | ||||||||
| |||||||||
| Glycosyl hydrolases family 2, TIM barrel domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 human beta-glucuronidase at 2.6 a resolution | |||||||||
| Identifiers | |||||||||
| Symbol | Glyco_hydro_2_C | ||||||||
| Pfam | PF02836 | ||||||||
| Pfam clan | CL0058 | ||||||||
| InterPro | IPR006103 | ||||||||
| PROSITE | PDOC00531 | ||||||||
| SCOP2 | 1bgl / SCOPe / SUPFAM | ||||||||
| CAZy | GH2 | ||||||||
| |||||||||
In molecular biology, Glycoside hydrolase family 2 is a family of glycoside hydrolases.
Glycoside hydrolases EC 3.2.1. 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(http://www.cazy.org/GH1.html) web site,[4] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[5]
Glycoside hydrolase family 2[6] 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,[7] in Escherichia coli lacZ (P00722), 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.[8] The sugar binding domain of these proteins has a jelly-roll fold.[8] These enzymes also include an immunoglobulin-like beta-sandwich domain.[8]
External links
References
- ^ Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7090–7094. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375.
- ^ Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
- ^ Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
- ^ Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
- ^ CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
- ^ Withers S. "Glycoside Hydrolase Family 2 (GH_2)". CAZypedia - carbohydrate active enzymes. Retrieved 2010-10-10.
- ^ Aebersold R, Withers SG, Gebler JC (1992). "Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli". J. Biol. Chem. 267 (16): 11126–11130. PMID 1350782.
- ^ a b c Matthews BW, Jacobson RH, Zhang XJ, DuBose RF (1994). "Three-dimensional structure of beta-galactosidase from E. coli". Nature. 369 (6483): 761–766. doi:10.1038/369761a0. PMID 8008071.