| 词条 | Autolysin |
| 释义 |
| Name = Gametolysin | EC_number = 3.4.24.38 | CAS_number = 97089-74-2 | IUBMB_EC_number = 3/4/24/38 | GO_code = | image = | width = | caption = }} An autolysin is an enzyme ({{EC number|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 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] References1. ^{{cite journal | vauthors = Jaenicke L, Kuhne W, Spessert R, Wahle U, Waffenschmidt S | title = Cell-wall lytic enzymes (autolysins) of Chlamydomonas reinhardtii are (hydroxy)proline-specific proteases | journal = European Journal of Biochemistry | volume = 170 | issue = 1–2 | pages = 485–91 | date = December 1987 | pmid = 3319620 | doi = 10.1111/j.1432-1033.1987.tb13725.x }} 2. ^{{cite journal | vauthors = Buchanan MJ, Imam SH, Eskue WA, Snell WJ | title = 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 | journal = The Journal of Cell Biology | volume = 108 | issue = 1 | pages = 199–207 | date = January 1989 | pmid = 2910877 | pmc = 2115355 | doi = 10.1083/jcb.108.1.199 }} 3. ^{{cite book | chapter = Gametolysin | title = Handbook of Proteolytic Enzymes | vauthors = Matsuda Y | year = 1998 |volume = |pages = 1140–1143 | editors = Barrett AJ, Rawlings ND, Woessner JF |edition = |publisher = Academic Press |location = London }} 4. ^{{cite journal | vauthors = Smith TJ, Blackman SA, Foster SJ | title = Autolysins of Bacillus subtilis: multiple enzymes with multiple functions | journal = Microbiology | volume = 146 ( Pt 2) | issue = 146 | pages = 249–62 | date = February 2000 | pmid = 10708363 | doi = 10.1099/00221287-146-2-249 }} External links
2 : EC 3.4.24|Bacterial enzymes |
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