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InterPro: IPR000974 Glycoside hydrolase, family 22, lysozyme

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UniProtKB
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338 proteins
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IPR000974 Glyco_hydro_22_lys
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Family
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Parent IPR001916 Glycoside hydrolase, family 22
Contains IPR019799 Glycoside hydrolase, family 22, conserved site
GO Term annotationHelp
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Process GO:0016998 cell wall macromolecule catabolic process
Function GO:0003796 lysozyme activity
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.

Lysozyme is a muramidase that hydrolyses beta-1,4-links between N-acetyl- muramic acid and N-acetyl-D-glucosamine in the peptidoglycan of bacterial cell walls [5], thus helping to fight invading bacteria. In this capacity, the enzyme is found in tears and saliva, but it has also been recruited for a digestive role in the true stomach (abomasum) of ruminants and colobine monkeys: here it probably degrades the cell walls of bacteria passing from the foregut, allowing the breakdown products to be digested by other stomach enzymes [6, 7]. The stomach form of lysozyme is endowed with special physiochemical properties that allow it to function in an acidic and protease-rich environment.

Lysozyme C is similar to alpha-lactalbumin in terms of primary sequence and structure [8], and both have probably evolved from a common ancestral protein. There is, however, no similarity in function, lactalbumin being involved in the formation of lactose and is essential for milk production. Another significant difference between the two enzymes is that while all lactalbumins have the ability to bind calcium, this property is restricted to only a few lysozymes [9].
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132l , 133l , 134l , 135l , 193l , 194l , 1a2y , 1aki , 1at5 , 1at6 , 1azf , 1b0d , 1b2k , 1b5u , 1b5v , 1b5w , 1b5x , 1b5y , 1b5z , 1b7l , 1b7m , 1b7n , 1b7o , 1b7p , 1b7q , 1b7r , 1b7s , 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 , 1fbi , 1fdl , 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 , 1hhl , 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 , 1op9 , 1oua , 1oub , 1ouc , 1oud , 1oue , 1ouf , 1oug , 1ouh , 1oui , 1ouj , 1p2c , 1ps5 , 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 , 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 , 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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Enzyme: EC:3.2.1.17
CAZy: GH22
Blocks: IPB000974

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Overlapping InterPro entriesHelp
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IPR000974 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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P00698 Lysozyme C

P08905 Lysozyme C-2

P29615 Lysozyme P

P48816 Lysozyme

P61626 Lysozyme C

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
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. Chung LP, Keshav S, Gordon S.
Cloning the human lysozyme cDNA: inverted Alu repeat in the mRNA and in situ hybridization for macrophages and Paneth cells.
Proc. Natl. Acad. Sci. U.S.A. 85 6227-31 1988 [PubMed: 3413092]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=3413092&action=stream&blobtype=pdf
6. Stewart CB, Schilling JW, Wilson AC.
Adaptive evolution in the stomach lysozymes of foregut fermenters.
Nature 330 401-4 1987 [PubMed: 3120013]
http://dx.doi.org/10.1038/330401a0
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. 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
9. 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
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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
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]
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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