Biology:Glycoside hydrolase family 53

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Glycosyl hydrolase family 53
PDB 1fob EBI.jpg
crystal structure of beta-1,4-galactanase from aspergillus aculeatus at 100k
Identifiers
SymbolGlyco_hydro_53
PfamPF07745
Pfam clanCL0058
InterProIPR011683
SCOP21fob / SCOPe / SUPFAM
OPM superfamily117
OPM protein1hjq
CAZyGH53

In molecular biology, the glycoside hydrolase family 53 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]

These enzymes are endo-1,4- beta-galactanases EC 3.2.1.89. The structure of this domain is known [8] and has a TIM barrel fold.

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 53" (in en). http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_53. 
  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. "Aspergillus aculeatus beta-1,4-galactanase: substrate recognition and relations to other glycoside hydrolases in clan GH-A". Biochemistry 41 (51): 15135–43. December 2002. doi:10.1021/bi026238c. PMID 12484750. 
This article incorporates text from the public domain Pfam and InterPro: IPR011683