spacer
spacer

Jump to: InterProScan Databases Documentation FTP site Help Advanced search

InterPro: IPR001329 Glycoside hydrolase, family 56, allergen Api/Dol m 2

Protein matchesHelp
UniProtKB
Matches:
30 proteins
AccessionHelp IPR001329 Glyco_hydro_56_Api/Dol
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR001968 Glycoside hydrolase, family 56
Contains IPR013785 Aldolase-type TIM barrel
IPR017853 Glycoside hydrolase, catalytic core
GO Term annotationHelp
Process GO:0006952 defense response
Function GO:0004415 hyalurononglucosaminidase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

O-Glycosyl 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 glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [1, 2, 3]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site [4]. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in clans.

Family 56 (GH56) encompasses a group of hyaluronidases (EC:3.2.1.35) that includes venom hyaluronidases [5] and mammalian sperm surface proteins (PH-20).

Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee King T.P., Hoffmann D., Loewenstein H., Marsh D.G., Platts-Mills T.A.E., Thomas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed of the first three letters of the genus; a space; the first letter of the species name; a space and an arabic number. In the event that two species names have identical designations, they are discriminated from one another by adding one or more letters (as necessary) to each species designation.

The allergens in this family include allergens with the following designations: Api m 2, Dol m 2 and Ves v 2.

The venom of Apis mellifera (honeybee) contains several biologically-active peptides and two enzymes, one of which is a hyaluronidase [5]. The amino acid sequence of bee venom hyaluronidase contains 349 amino acids, and includes four cysteines and a number of potential glycosylation sites [5]. The sequence shows a high degree of similarity to PH-20, a membrane protein of mammalian sperm involved in sperm-egg adhesion, supporting the view that hyaluronidases play a role in fertilisation [5].

Structural linksHelp
SCOP: c.1.8.9
CATH: 3.20.20.70
Database linksHelp
Enzyme: EC:3.2.1.35
CAZy: GH56
Blocks: IPB001329

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001329 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P49370 Hyaluronidase A

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013785 Aldolase-type TIM barrel
IPR017853 Glycoside hydrolase, catalytic core
IPR001329 Glycoside hydrolase, family 56, allergen Api/Dol m 2
IPR001968 Glycoside hydrolase, family 56
IPR018155 Hyaluronidase
PDB Chain
ModBase
CATH Domain

PublicationsHelp
1. Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G.
Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.
Proc. Natl. Acad. Sci. U.S.A. 92 7090-4 1995 [PubMed: 7624375]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7624375&action=stream&blobtype=pdf
2. Davies G, Henrissat B.
Structures and mechanisms of glycosyl hydrolases.
Structure 3 853-9 1995 [PubMed: 8535779]
http://dx.doi.org/10.1016/S0969-2126(01)00220-9
3. Bairoch A.
Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT.
1999
4. Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999
5. Gmachl M, Kreil G.
Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm.
Proc. Natl. Acad. Sci. U.S.A. 90 3569-73 1993 [PubMed: 7682712]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=7682712

Additional ReadingHelp
Padavattan S, Schirmer T, Schmidt M, Akdis C, Valenta R, Mittermann I, Soldatova L, Slater J, Mueller U, Markovic-Housley Z.
Identification of a B-cell epitope of hyaluronidase, a major bee venom allergen, from its crystal structure in complex with a specific Fab.
J. Mol. Biol. 368 2007 742-52 [PubMed: 17374540]
http://dx.doi.org/10.1016/j.jmb.2007.02.036
Markovic-Housley Z, Miglierini G, Soldatova L, Rizkallah PJ, Muller U, Schirmer T.
Crystal structure of hyaluronidase, a major allergen of bee venom.
Structure 8 2000 1025-35 [PubMed: 11080624]
http://dx.doi.org/10.1016/S0969-2126(00)00511-6
Skov LK, Seppala U, Coen JJ, Crickmore N, King TP, Monsalve R, Kastrup JS, Spangfort MD, Gajhede M.
Structure of recombinant Ves v 2 at 2.0 Angstrom resolution: structural analysis of an allergenic hyaluronidase from wasp venom.
Acta Crystallogr. D Biol. Crystallogr. 62 2006 595-604 [PubMed: 16699186]
http://dx.doi.org/10.1107/S0907444906010687
el Hassouni M, Henrissat B, Chippaux M, Barras F.
Nucleotide sequences of the arb genes, which control beta-glucoside utilization in Erwinia chrysanthemi: comparison with the Escherichia coli bgl operon and evidence for a new beta-glycohydrolase family including enzymes from eubacteria, archeabacteria, and humans.
J. Bacteriol. 174 1992 765-77 [PubMed: 1732212]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=1732212&action=stream&blobtype=pdf
spacer
spacer
InterPro 23.1