Biology:Glycoside hydrolase family 2

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Short description: Enzyme group
Glycosyl hydrolases family 2, sugar binding domain
PDB 1jz3 EBI.jpg
e. coli (lacz) beta-galactosidase-trapped 2-deoxy-galactosyl enzyme intermediate
Identifiers
SymbolGlyco_hydro_2_N
PfamPF02837
Pfam clanCL0202
InterProIPR006104
PROSITEPDOC00531
SCOP21bgl / SCOPe / SUPFAM
CAZyGH2
Glycosyl hydrolases family 2
PDB 1jz3 EBI.jpg
e. coli (lacz) beta-galactosidase-trapped 2-deoxy-galactosyl enzyme intermediate
Identifiers
SymbolGlyco_hydro_2
PfamPF00703
InterProIPR006102
PROSITEPDOC00531
SCOP21bgl / SCOPe / SUPFAM
CAZyGH2
Glycosyl hydrolases family 2, TIM barrel domain
PDB 1bhg EBI.jpg
human beta-glucuronidase at 2.6 a resolution
Identifiers
SymbolGlyco_hydro_2_C
PfamPF02836
Pfam clanCL0058
InterProIPR006103
PROSITEPDOC00531
SCOP21bgl / SCOPe / SUPFAM
CAZyGH2

In molecular biology, Glycoside hydrolase family 2 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 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 (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.[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

References

  1. "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. doi:10.1073/pnas.92.15.7090. PMID 7624375. Bibcode1995PNAS...92.7090H. 
  2. "Structures and mechanisms of glycosyl hydrolases". Structure 3 (9): 853–9. September 1995. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779. 
  3. "Updating the sequence-based classification of glycosyl hydrolases". The Biochemical Journal 316 (Pt 2): 695–6. June 1996. doi:10.1042/bj3160695. PMID 8687420. 
  4. "Home" (in en). http://www.cazy.org/. 
  5. "The carbohydrate-active enzymes database (CAZy) in 2013". Nucleic Acids Research 42 (Database issue): D490-5. January 2014. doi:10.1093/nar/gkt1178. PMID 24270786. 
  6. "Glycoside Hydrolase Family 2" (in en). http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_2. 
  7. CAZypedia Consortium (December 2018). "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes". Glycobiology 28 (1): 3–8. doi:10.1093/glycob/cwx089. PMID 29040563. https://hal.archives-ouvertes.fr/hal-01886461/file/Hehemann_2018_01.pdf. 
  8. Withers S. "Glycoside Hydrolase Family 2 (GH_2)". CAZypedia - carbohydrate active enzymes. http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_2. 
  9. "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. doi:10.1016/S0021-9258(19)49884-0. PMID 1350782. 
  10. 10.0 10.1 10.2 "Three-dimensional structure of beta-galactosidase from E. coli". Nature 369 (6483): 761–6. June 1994. doi:10.1038/369761a0. PMID 8008071. Bibcode1994Natur.369..761J. 
This article incorporates text from the public domain Pfam and InterPro: IPR006102
This article incorporates text from the public domain Pfam and InterPro: IPR006103
This article incorporates text from the public domain Pfam and InterPro: IPR006104