Autolysin: Difference between revisions
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{{Infobox enzyme |
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| Name = Gametolysin |
| Name = Gametolysin |
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| EC_number = 3.4.24.38 |
| EC_number = 3.4.24.38 |
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Revision as of 12:11, 27 February 2020
| Gametolysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.38 | ||||||||
| CAS no. | 97089-74-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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An autolysin is an enzyme (EC 3.4.24.38, gametolysin, Chlamydomonas cell wall degrading protease, lysin, Chlamydomonas reinhardtii metalloproteinase, gamete lytic enzyme, gamete autolysin) that hydrolyzes (and breaks down) the components of a biological cell or a tissue in which it is produced.[1][2][3] It is similar in function to a lysozyme. This enzyme catalyses the following chemical reaction
- Cleavage of the proline- and hydroxyproline-rich proteins of the Chlamydomonas cell wall; also cleaves azocasein, gelatin and Leu-Trp-Met-Arg-Phe-Ala
This glycoprotein is present in Chlamydomonas reinhardtii gametes.
Autolysins (not necessarily having this specific catalytic activity of EC 3.4.24.38) exist in all bacteria containing peptidoglycan. The peptidoglycan matrix is very rigid, so these enzymes break down the peptidoglycan matrix in small sections so that growth and division of cells can occur. Autolysins do this by hydrolyzing the β-(1,4) bond between N-acetylmuramic acid and N-acetylglucosamine molecules. Autolysins are naturally produced by peptidoglycan containing bacteria, but excessive amounts will degrade the peptidoglycan matrix and cause the cell to burst due to osmotic pressure. Gram-positive bacteria regulate autolysins with teichoic acid molecules attached to the tetrapeptide of the peptidoglycan matrix.[4]
The antibiotics complestatin and corbomycin prevent autolysin from remodeling the cell wall by binding to peptidoglycan, therefore stopping bacterial growth.[5]
References
- ^ Jaenicke L, Kuhne W, Spessert R, Wahle U, Waffenschmidt S (December 1987). "Cell-wall lytic enzymes (autolysins) of Chlamydomonas reinhardtii are (hydroxy)proline-specific proteases". European Journal of Biochemistry. 170 (1–2): 485–91. doi:10.1111/j.1432-1033.1987.tb13725.x. PMID 3319620.
- ^ Buchanan MJ, Imam SH, Eskue WA, Snell WJ (January 1989). "Activation of the cell wall degrading protease, lysin, during sexual signalling in Chlamydomonas: the enzyme is stored as an inactive, higher relative molecular mass precursor in the periplasm". The Journal of Cell Biology. 108 (1): 199–207. doi:10.1083/jcb.108.1.199. PMC 2115355. PMID 2910877.
- ^ Matsuda Y (1998). "Gametolysin". Handbook of Proteolytic Enzymes. London: Academic Press. pp. 1140–1143.
{{cite book}}: Unknown parameter|editors=ignored (|editor=suggested) (help) - ^ Smith TJ, Blackman SA, Foster SJ (February 2000). "Autolysins of Bacillus subtilis: multiple enzymes with multiple functions". Microbiology. 146 ( Pt 2) (146): 249–62. doi:10.1099/00221287-146-2-249. PMID 10708363.
- ^ Culp, Elizabeth J.; Waglechner, Nicholas; Wang, Wenliang; Fiebig-Comyn, Aline A.; Hsu, Yen-Pang; Koteva, Kalinka; Sychantha, David; Coombes, Brian K.; Van Nieuwenhze, Michael S.; Brun, Yves V.; Wright, Gerard D. (2020). "Evolution-guided discovery of antibiotics that inhibit peptidoglycan remodelling". Nature. 578 (7796): 582–587. doi:10.1038/s41586-020-1990-9. ISSN 0028-0836.
External links
- Gametolysin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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