 |
InterPro: IPR001329 Glycoside hydrolase, family 56, allergen Api/Dol m 2
Protein matches
|
UniProtKB Matches: 30 proteins |
|
Accession
|
IPR001329 Glyco_hydro_56_Api/Dol |
Type
|
Family |
Signatures
|
|
InterPro Relationships
|
|
Parent
|
IPR001968 Glycoside hydrolase, family 56
|
|
Contains
|
IPR013785 Aldolase-type TIM barrel
IPR017853 Glycoside hydrolase, catalytic core
|
GO Term annotation
|
|
Process
|
GO:0006952 defense response
|
|
Function
|
GO:0004415 hyalurononglucosaminidase activity
|
|
InterPro annotation
|
|
Entry Details in BioMart
|
Abstract
|
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 links
|
|
Database links
|
|
Additional Reading
|
|
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
|
|
|
InterPro 23.1
|