Glycoside hydrolase family 79

Glycosyl hydrolase family 79, N-terminal domain
Identifiers
Symbol	Glyco_hydro_79n
Pfam	PF03662
Pfam clan	CL0058
InterPro	IPR005199
CAZy	GH79
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In molecular biology, glycoside hydrolase family 79 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 79 includes endo-beta-N-glucuronidase EC 3.2.1.31 and heparanase (CAZY GH_79). Heparan sulphate proteoglycans (HSPGs) play a key role in the self- assembly, insolubility and barrier properties of basement membranes and extracellular matrices. Hence, cleavage of heparan sulphate (HS) affects the integrity and functional state of tissues and thereby fundamental normal and pathological phenomena involving cell migration and response to changes in the extracellular microenvironment. Heparanase degrades HS at specific intrachain sites. The enzyme is synthesized as a latent approximately 65 kDa protein that is processed at the N-terminus into a highly active approximately 50 kDa form. Experimental evidence suggests that heparanase may facilitate both tumour cell invasion and neovascularisation, both critical steps in cancer progression. The enzyme is also involved in cell migration associated with inflammation and autoimmunity. ^[8]

References

1. Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G (July 1995). "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. Bibcode:1995PNAS...92.7090H. doi: 10.1073/pnas.92.15.7090 . PMC   41477 . PMID   7624375.
2. Davies G, Henrissat B (September 1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–9. doi: 10.1016/S0969-2126(01)00220-9 . PMID   8535779.
3. Henrissat B, Bairoch A (June 1996). "Updating the sequence-based classification of glycosyl hydrolases". The Biochemical Journal. 316 ( Pt 2) (Pt 2): 695–6. doi:10.1042/bj3160695. PMC   1217404 . PMID   8687420.
4. "Home". CAZy.org. Retrieved 2018-03-06.
5. Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, Henrissat B (January 2014). "The carbohydrate-active enzymes database (CAZy) in 2013". Nucleic Acids Research. 42 (Database issue): D490–5. doi:10.1093/nar/gkt1178. PMC   3965031 . PMID   24270786.
6. "Glycoside Hydrolase Family 79". CAZypedia.org. Retrieved 2018-03-06.
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 . hdl:21.11116/0000-0003-B7EB-6. PMID   29040563.
8. Vlodavsky I, Goldshmidt O, Zcharia E, Metzger S, Chajek-shaul T, Atzmon R, Guatta-rangini Z, Friedmann Y (2001). "Molecular properties and involvement of heparanase in cancer progression and normal development". Biochimie. 83 (8): 831–839. doi:10.1016/S0300-9084(01)01318-9. PMID   11530216.

This article incorporates text from the public domain Pfam and InterPro: IPR005199