Biology:Glycoside hydrolase family 20

From HandWiki
Glycosyl hydrolase family 20, catalytic domain
PDB 1m01 EBI.jpg
wildtype streptomyces plicatus beta-hexosaminidase in complex with product (glcnac)
Identifiers
SymbolGlyco_hydro_20
PfamPF00728
Pfam clanCL0058
InterProIPR015883
SCOP21qba / SCOPe / SUPFAM
CAZyGH20
CDDcd02742
Glycosyl hydrolase family 20, domain 2
PDB 2gjx EBI.jpg
crystallographic structure of human beta-hexosaminidase a
Identifiers
SymbolGlyco_hydro_20b
PfamPF02838
InterProIPR015882
SCOP21qba / SCOPe / SUPFAM
CAZyGH20

In molecular biology, glycoside hydrolase family 20 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 web site,[4][5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[6][7]

Glycoside hydrolase family 20 CAZY GH_20 comprises enzymes with several known activities; beta-hexosaminidase (EC 3.2.1.52); lacto-N-biosidase (EC 3.2.1.140). Carbonyl oxygen of the C-2 acetamido group of the substrate acts as the catalytic nucleophile/base in this family of enzymes.

In the brain and other tissues, beta-hexosaminidase A degrades GM2 gangliosides; specifically, the enzyme hydrolyses terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. There are 3 forms of beta-hexosaminidase: hexosaminidase A is a trimer, with one alpha, one beta-A and one beta-B chain; hexosaminidase B is a tetramer of two beta-A and two beta-B chains; and hexosaminidase S is a homodimer of alpha chains. The two beta chains are derived from the cleavage of a precursor. Mutations in the beta-chain lead to Sandhoff disease, a lysosomal storage disorder characterised by accumulation of GM2 ganglioside.[8]

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 20" (in en). http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_20. 
  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. "Molecular basis of an adult form of Sandhoff disease: substitution of glutamine for arginine at position 505 of the beta-chain of beta-hexosaminidase results in a labile enzyme". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1182 (2): 142–6. September 1993. doi:10.1016/0925-4439(93)90134-m. PMID 8357844. 
This article incorporates text from the public domain Pfam and InterPro: IPR015883