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PROSITE documentation PDOC51909

Invertebrate (I)-type lysozyme domain profile





Description

Lysozyme (EC 3.2.1.17) is an ubiquitous enzyme and is widely distributed in a range of phylogenetically diverse organisms from bacteriophage to humans. Lysozyme is mainly involved in the innate immune system and protection of host against microbial infection. The mechanism of lysozyme in killing bacteria is by hydrolyzing the β-1,4-glycosidic linkages between N-acetyl muramic acid (NAM) and N-acetyl glucosamine (NAG) of peptidoglycan (PG), which is a layer in the bacterial cell wall. Based on differences in amino acid sequences, catalytic characteristic, and original sources, lysozymes are classified into chicken (C)-type (see <PDOC00119>), goose (G)-type, virus (V)-type, lambda (L)-type, chalaropsis (Ch)-type (see <PDOC00737>), plant (P)-type and invertebrate (I)-type. I-type lysozymes have been identified in phylogenetically diverse organisms, including mollusca, nematoda, annelida, arthropoda and echinodermata. I-type lysozymes play an important role in immunity and digestion in invertebrates and are usually regarded as the first barrier against pathogens. The I-type lysozyme has multiple activities. For its muramidase activity, it is identified as lysozyme; for its isopeptidase activity, it is named destabilase; chitinase and non-enzymatic antibacterial activities are also manifested [1,2,3,4,5]. They belong to the glycosyl hydrolase 22 (GH22) family [E1].

The I-type lysozyme domain is characterized by six α-helices and one β-sheet (see <PDB:2DQA>). It contains 14 cysteines that all form disulfide bonds (C1-C12, C2-C14, C3-C4, C5-C6, C7-C10, C8-C9, C11-C13). The catalytic residues are a glutamate in the α1-helix and an aspartate in the β1-strand [6,7].

The profile we developed covers the entire I-type lysozyme domain.

Last update:

October 2019 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

LYSOZYME_I, PS51909; Invertebrate (I)-type lysozyme domain profile  (MATRIX)


References

1AuthorsBachali S. Bailly X. Jolles J. Jolles P. Deutsch J.S.
TitleThe lysozyme of the starfish Asterias rubens. A paradygmatic type i lysozyme.
SourceEur. J. Biochem. 271:237-242(2004).
PubMed ID14717691
DOI10.1046/j.1432-1033.2003.03915.x

2AuthorsSchulenburg H. Boehnisch C.
TitleDiversification and adaptive sequence evolution of Caenorhabditis lysozymes (Nematoda: Rhabditidae).
SourceBMC Evol. Biol. 8:114-114(2008).
PubMed ID29807121
DOI10.1016/j.fsi.2018.05.037

3AuthorsZhang H.-W. Sun C. Sun S.-S. Zhao X.-F. Wang J.-X.
TitleFunctional analysis of two invertebrate-type lysozymes from red swamp crayfish, Procambarus clarkii.
SourceFish. Shellfish. Immunol. 29:1066-1072(2010).
PubMed ID20816803
DOI10.1016/j.fsi.2010.08.023

4AuthorsRen Q. Qi Y.-L. Hui K.-M. Zhang Z. Zhang C.-Y. Wang W.
TitleFour invertebrate-type lysozyme genes from triangle-shell pearl mussel (Hyriopsis cumingii).
SourceFish. Shellfish. Immunol. 33:909-915(2012).
PubMed ID22884462
DOI10.1016/j.fsi.2012.07.019

5AuthorsChen F. Wei Z. Zhao X. Shao Y. Zhang W.
TitleMolecular characteristics, expression, and antimicrobial activities of i-type lysozyme from the razor clam Sinonovacula constricta.
SourceFish. Shellfish. Immunol. 79:321-326(2018).

6AuthorsGoto T. Abe Y. Kakuta Y. Takeshita K. Imoto T. Ueda T.
TitleCrystal structure of Tapes japonica Lysozyme with substrate analogue: structural basis of the catalytic mechanism and manifestation of its chitinase activity accompanied by quaternary structural change.
SourceJ. Biol. Chem. 282:27459-27467(2007).
PubMed ID17631496
DOI10.1074/jbc.M704555200

7AuthorsKuwano Y. Yoneda K. Kawaguchi Y. Araki T.
TitleThe tertiary structure of an i-type lysozyme isolated from the common orient clam (Meretrix lusoria).
SourceActa Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 69:1202-1206(2013).
PubMed ID24192349
DOI10.1107/S1744309113028170

E1Sourcehttp://www.cazy.org/GH22.html



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