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3  structures 99  species 0  interactions 293  sequences 9  architectures

Family: Glyco_hydro_79n (PF03662)

Summary: Glycosyl hydrolase family 79, N-terminal domain

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This is the Wikipedia entry entitled "Glycoside hydrolase family 79". More...

Glycoside hydrolase family 79 Edit Wikipedia article

Glycosyl hydrolase family 79, N-terminal domain
Identifiers
Symbol Glyco_hydro_79n
Pfam PF03662
Pfam clan CL0058
InterPro IPR005199
CAZy GH79

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(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 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.[6]

References[edit]

  1. ^ 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. 
  2. ^ 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. 
  3. ^ Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
  4. ^ Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
  5. ^ CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
  6. ^ 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

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Glycosyl hydrolase family 79, N-terminal domain Provide feedback

Family of endo-beta-N-glucuronidase, or heparanase. Heparan sulfate proteoglycans (HSPGs) play a key role in the self- assembly, insolubility and barrier properties of basement membranes and extracellular matrices. Hence, cleavage of heparan sulfate (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 micro-environment. Heparanase degrades HS at specific intra-chain sites. The enzyme is synthesised 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 neovascularization, both critical steps in cancer progression. The enzyme is also involved in cell migration associated with inflammation and autoimmunity [1].

Literature references

  1. Vlodavsky I, Goldshmidt O, Zcharia E, Metzger S, Chajek-Shaul T, Atzmon R, Guatta-Rangini Z, Friedmann Y; , Biochimie 2001;83:831-839.: Molecular properties and involvement of heparanase in cancer progression and normal development. PUBMED:11530216 EPMC:11530216


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR005199

O-Glycosyl hydrolases (EC) 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 glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [PUBMED:7624375, PUBMED:8535779]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site.

This is a family of endo-beta-N-glucuronidase, or heparanase belonging to glycoside hydrolase family 79 (CAZY). 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 tumor cell invasion and neovascularization, both critical steps in cancer progression. The enzyme is also involved in cell migration associated with inflammation and autoimmunity [PUBMED:11530216].

Gene Ontology

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Domain organisation

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  Seed
(9)
Full
(293)
Representative proteomes NCBI
(323)
Meta
(6)
RP15
(43)
RP35
(82)
RP55
(120)
RP75
(160)
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  Seed
(9)
Full
(293)
Representative proteomes NCBI
(323)
Meta
(6)
RP15
(43)
RP35
(82)
RP55
(120)
RP75
(160)
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External links

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Seed source: CAZY
Previous IDs: none
Type: Domain
Author: Finn RD
Number in seed: 9
Number in full: 293
Average length of the domain: 232.70 aa
Average identity of full alignment: 31 %
Average coverage of the sequence by the domain: 49.33 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.5 20.5
Trusted cut-off 20.7 20.7
Noise cut-off 19.7 20.4
Model length: 320
Family (HMM) version: 9
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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Glyco_hydro_79n domain has been found. There are 3 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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