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InterPro: IPR019799 Glycoside hydrolase, family 22, conserved site

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495 proteins
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IPR019799 Glyco_hydro_22_CS
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Conserved_site
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Found in IPR000545 Lactalbumin
IPR000974 Glycoside hydrolase, family 22, lysozyme
IPR001916 Glycoside hydrolase, family 22
InterPro annotation
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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.

Glycoside hydrolase family 22 GH22 comprises enzymes with two known activities; lysozyme type C (EC:3.2.1.17) and alpha-lactalbumins. Asp and/or the carbonyl oxygen of the C-2 acetamido group of the substrate acts as the catalytic nucleophile/base.

Alpha-lactalbumin [5, 6] is a milk protein that acts as the regulatory subunit of lactose synthetase, acting to promote the conversion of galactosyltransferase to lactose synthase, which is essential for milk production. In the mammary gland, alpha-lactalbumin changes the substrate specificity of galactosyltransferase from N-acetylglucosamine to glucose.

Lysozymes (EC:3.2.1.17) act as bacteriolytic enzymes by hydrolyzing the beta(1->4) bonds between N-acetylglucosamine and N-acetylmuramic acid in the peptidoglycan of prokaryotic cell walls. It has also been recruited for a digestive role in certain ruminants and colobine monkeys [7]. There are at least five different classes of lysozymes [8]: C (chicken type), G (goose type), phage-type (T4), fungi (Chalaropsis), and bacterial (Bacillus subtilis). There are few similarities in the sequences of the different types of lysozymes.

Lysozyme type C and alpha-lactalbumin are similar both in terms of primary sequence and structure, and probably evolved from a common ancestral protein [9]. Around 35 to 40% of the residues are conserved in both proteins as well as the positions of the four disulphide bonds. There is, however, no similarity in function. Another significant difference between the two enzymes is that all lactalbumins have the ability to bind calcium [10], while this property is restricted to only a few lysozymes [11].

The binding site was deduced using high resolution X-ray structure analysis and was shown to consist of three aspartic acid residues. It was first suggested that calcium bound to lactalbumin stabilised the structure, but recently it has been claimed that calcium controls the release of lactalbumin from the golgi membrane and that the pattern of ion binding may also affect the catalytic properties of the lactose synthetase complex.

The pattern for this entry includes three cysteines which are involved in two of the disulphide bonds found in these proteins.
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132l , 133l , 134l , 135l , 193l , 194l , 1a2y , 1a4v , 1aki , 1alc , 1at5 , 1at6 , 1azf , 1b0d , 1b2k , 1b5u , 1b5v , 1b5w , 1b5x , 1b5y , 1b5z , 1b7l , 1b7m , 1b7n , 1b7o , 1b7p , 1b7q , 1b7r , 1b7s , 1b9o , 1bb3 , 1bb4 , 1bb5 , 1bb6 , 1bb7 , 1bgi , 1bhz , 1bql , 1bvk , 1bvx , 1bwh , 1bwi , 1bwj , 1c08 , 1c10 , 1c43 , 1c45 , 1c46 , 1c7p , 1cj6 , 1cj7 , 1cj8 , 1cj9 , 1ckc , 1ckd , 1ckf , 1ckg , 1ckh , 1d6p , 1d6q , 1di3 , 1di4 , 1di5 , 1dkj , 1dkk , 1dpw , 1dpx , 1dqj , 1dzb , 1e8l , 1el1 , 1eq4 , 1eq5 , 1eqe , 1f0w , 1f10 , 1f6r , 1f6s , 1fbi , 1fdl , 1fkq , 1fkv , 1flq , 1flu , 1flw , 1fly , 1fn5 , 1g7h , 1g7i , 1g7j , 1g7l , 1g7m , 1gay , 1gaz , 1gb0 , 1gb2 , 1gb3 , 1gb5 , 1gb6 , 1gb7 , 1gb8 , 1gb9 , 1gbo , 1gbw , 1gbx , 1gby , 1gbz , 1gd6 , 1gdw , 1gdx , 1ge0 , 1ge1 , 1ge2 , 1ge3 , 1ge4 , 1gev , 1gez , 1gf0 , 1gf3 , 1gf4 , 1gf5 , 1gf6 , 1gf7 , 1gf8 , 1gf9 , 1gfa , 1gfe , 1gfg , 1gfh , 1gfj , 1gfk , 1gfr , 1gft , 1gfu , 1gfv , 1ghl , 1gpq , 1gwd , 1gxv , 1gxx , 1h6m , 1h87 , 1hc0 , 1hel , 1hem , 1hen , 1heo , 1hep , 1heq , 1her , 1hew , 1hf4 , 1hfx , 1hfy , 1hfz , 1hhl , 1hmk , 1hml , 1hnl , 1hsw , 1hsx , 1i1z , 1i20 , 1i22 , 1i56 , 1ic4 , 1ic5 , 1ic7 , 1iee , 1iiz , 1inu , 1ioc , 1ioq , 1ior , 1ios , 1iot , 1ip1 , 1ip2 , 1ip3 , 1ip4 , 1ip5 , 1ip6 , 1ip7 , 1ir7 , 1ir8 , 1ir9 , 1ivm , 1iwt , 1iwu , 1iwv , 1iww , 1iwx , 1iwy , 1iwz , 1ix0 , 1iy3 , 1iy4 , 1j1o , 1j1p , 1j1x , 1ja2 , 1ja4 , 1ja6 , 1ja7 , 1jef , 1jhl , 1jis , 1jit , 1jiy , 1jj0 , 1jj1 , 1jj3 , 1jka , 1jkb , 1jkc , 1jkd , 1jpo , 1jse , 1jsf , 1jto , 1jtp , 1jtt , 1jug , 1jwr , 1kip , 1kiq , 1kir , 1kxw , 1kxx , 1kxy , 1laa , 1lcn , 1lhh , 1lhi , 1lhj , 1lhk , 1lhl , 1lhm , 1lj3 , 1lj4 , 1lje , 1ljf , 1ljg , 1ljh , 1lji , 1ljj , 1ljk , 1ljn , 1lkr , 1lks , 1lma , 1lmc , 1lmn , 1lmo , 1lmp , 1lmq , 1lmt , 1loz , 1lpi , 1lsa , 1lsb , 1lsc , 1lsd , 1lse , 1lsf , 1lsg , 1lsm , 1lsn , 1lsy , 1lsz , 1lyo , 1lys , 1lyy , 1lyz , 1lz1 , 1lz2 , 1lz4 , 1lz5 , 1lz6 , 1lz8 , 1lz9 , 1lza , 1lzb , 1lzc , 1lzd , 1lze , 1lzg , 1lzh , 1lzr , 1lzs , 1lzt , 1lzy , 1mel , 1mlc , 1n4f , 1nby , 1nbz , 1ndg , 1ndm , 1nf5 , 1nhe , 1nkh , 1nmm , 1nqi , 1nwg , 1o23 , 1op9 , 1oqm , 1oua , 1oub , 1ouc , 1oud , 1oue , 1ouf , 1oug , 1ouh , 1oui , 1ouj , 1p2c , 1ps5 , 1pzy , 1qio , 1qqy , 1qsw , 1qtk , 1rcm , 1re2 , 1rem , 1rex , 1rey , 1rez , 1rfp , 1ri8 , 1rjc , 1sf4 , 1sf6 , 1sf7 , 1sfb , 1sfg , 1sq2 , 1t3p , 1t6v , 1tay , 1tby , 1tcy , 1tdy , 1tew , 1ua6 , 1uac , 1ubz , 1uc0 , 1uco , 1uia , 1uib , 1uic , 1uid , 1uie , 1uif , 1uig , 1uih , 1uuz , 1v7s , 1v7t , 1vat , 1vau , 1vdp , 1vdq , 1vds , 1vdt , 1ved , 1vfb , 1w08 , 1w6z , 1wqm , 1wqn , 1wqo , 1wqp , 1wqq , 1wqr , 1wtm , 1wtn , 1xei , 1xej , 1xek , 1xfp , 1xft , 1xgp , 1xgq , 1yam , 1yan , 1yao , 1yap , 1yaq , 1yik , 1yil , 1ykx , 1yky , 1ykz , 1yl0 , 1yl1 , 1yqv , 1yro , 1z55 , 1zmy , 1zv5 , 1zvh , 1zvy , 207l , 208l , 2a6u , 2a7d , 2a7f , 2aub , 2b5z , 2blx , 2bly , 2bpu , 2bqa , 2bqb , 2bqc , 2bqd , 2bqe , 2bqf , 2bqg , 2bqh , 2bqi , 2bqj , 2bqk , 2bql , 2bqm , 2bqn , 2bqo , 2c8o , 2c8p , 2cds , 2cgi , 2cwi , 2d4i , 2d4j , 2d4k , 2d6b , 2d91 , 2dqc , 2dqd , 2dqe , 2dqf , 2dqg , 2dqh , 2dqi , 2dqj , 2eiz , 2eks , 2epe , 2eql , 2f2n , 2f30 , 2f4a , 2f4g , 2fbb , 2fbd , 2fyc , 2fyd , 2g4n , 2g4p , 2g4q , 2goi , 2gv0 , 2h5z , 2h9j , 2h9k , 2hea , 2heb , 2hec , 2hed , 2hee , 2hef , 2hs7 , 2hs9 , 2hso , 2htx , 2hu1 , 2hu3 , 2hub , 2i25 , 2i26 , 2i6z , 2iff , 2ihl , 2lhm , 2lym , 2lyo , 2lyz , 2lz2 , 2lzh , 2lzt , 2mea , 2meb , 2mec , 2med , 2mee , 2mef , 2meg , 2meh , 2mei , 2nwd , 2pc2 , 2q0m , 2vb1 , 2yss , 2yvb , 2z12 , 2z18 , 2z19 , 2z2e , 2zq3 , 2zq4 , 3b6l , 3b72 , 3d9a , 3ems , 3hfm , 3lhm , 3lym , 3lyo , 3lyt , 3lyz , 3lz2 , 3lzt , 4lym , 4lyo , 4lyt , 4lyz , 4lzt , 5lym , 5lyt , 5lyz , 6lyt , 6lyz , 7lyz , 8lyz
SCOP: d.2.1.2
CATH: 1.10.530.10

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Overlapping InterPro entriesHelp
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IPR019799 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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P00698 Lysozyme C

P00709 Alpha-lactalbumin

P08905 Lysozyme C-2

P29615 Lysozyme P

P48816 Lysozyme

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000545 Lactalbumin
IPR019799 Glycoside hydrolase, family 22, conserved site
IPR000974 Glycoside hydrolase, family 22, lysozyme
IPR001916 Glycoside hydrolase, family 22
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
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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. Shewale JG, Sinha SK, Brew K.
Evolution of alpha-lactalbumins. The complete amino acid sequence of the alpha-lactalbumin from a marsupial (Macropus rufogriseus) and corrections to regions of sequence in bovine and goat alpha-lactalbumins.
J. Biol. Chem. 259 4947-56 1984 [PubMed: 6715332]
http://intl.jbc.org/cgi/reprint/259/8/4947.pdf
6. Hall L, Campbell PN.
Alpha-lactalbumin and related proteins: a versatile gene family with an interesting parentage.
Essays Biochem. 22 1-26 1986 [PubMed: 3104032]
7. Irwin DM, Wilson AC.
Multiple cDNA sequences and the evolution of bovine stomach lysozyme.
J. Biol. Chem. 264 11387-93 1989 [PubMed: 2738070]
http://intl.jbc.org/cgi/content/abstract/264/19/11387
8. Kamei K, Hara S, Ikenaka T, Murao S.
Amino acid sequence of a lysozyme (B-enzyme) from Bacillus subtilis YT-25.
J. Biochem. 104 832-6 1988 [PubMed: 3148618]
http://jb.oxfordjournals.org/cgi/content/abstract/104/5/832
9. Nitta K, Sugai S.
The evolution of lysozyme and alpha-lactalbumin.
Eur. J. Biochem. 182 111-8 1989 [PubMed: 2731545]
http://dx.doi.org/10.1111/j.1432-1033.1989.tb14806.x
10. Stuart DI, Acharya KR, Walker NP, Smith SG, Lewis M, Phillips DC.
Alpha-lactalbumin possesses a novel calcium binding loop.
Nature 324 84-7 1986 [PubMed: 3785375]
http://dx.doi.org/10.1038/324084a0
11. Nitta K, Tsuge H, Sugai S, Shimazaki K.
The calcium-binding property of equine lysozyme.
FEBS Lett. 223 405-8 1987 [PubMed: 3666156]
http://dx.doi.org/10.1016/0014-5793(87)80328-9

Additional ReadingHelp
Open in usermanual
Henrissat B.
A classification of glycosyl hydrolases based on amino acid sequence similarities.
Biochem. J. 280 ( Pt 2) 1991 309-16 [PubMed: 1747104]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1747104
Pompidor G, D'Aleo A, Vicat J, Toupet L, Giraud N, Kahn R, Maury O.
Protein crystallography through supramolecular interactions between a lanthanide complex and arginine.
Angew. Chem. Int. Ed. Engl. 47 2008 3388-91 [PubMed: 18350532]
Mueller-Dieckmann C, Panjikar S, Schmidt A, Mueller S, Kuper J, Geerlof A, Wilmanns M, Singh RK, Tucker PA, Weiss MS.
On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths.
Acta Crystallogr. D Biol. Crystallogr. 63 2007 366-80 [PubMed: 17327674]
http://dx.doi.org/10.1107/S0907444906055624
Nakanishi T, Tsumoto K, Yokota A, Kondo H, Kumagai I.
Critical contribution of VH-VL interaction to reshaping of an antibody: the case of humanization of anti-lysozyme antibody, HyHEL-10.
Protein Sci. 17 2008 261-70 [PubMed: 18227432]
http://dx.doi.org/10.1110/ps.073156708
Nonaka Y, Aizawa T, Akieda D, Yasui M, Watanabe M, Watanabe N, Tanaka I, Kamiya M, Mizuguchi M, Demura M, Kawano K.
Spontaneous asparaginyl deamidation of canine milk lysozyme under mild conditions.
Proteins 72 2008 313-22 [PubMed: 18214981]
http://dx.doi.org/10.1002/prot.21927
Michaux C, Pouyez J, Wouters J, Prive GG.
Protecting role of cosolvents in protein denaturation by SDS: a structural study.
BMC Struct. Biol. 8 2008 29 [PubMed: 18522744]
http://dx.doi.org/10.1186/1472-6807-8-29
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