Autolysin

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 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]

References

↑ Jaenicke, L.; Kunhe, W.; Spessert, R.; Wahle, U.; Waffenschmidt, S. (1987). "Cell-wall lytic enzymes (autolysins) of Chlamydomonas reinhardtii are (hydroxy)proline-specific proteases". Eur. J. Biochem. 170: 485–491. doi:10.1111/j.1432-1033.1987.tb13725.x. PMID 3319620.
↑ Buchanan, M.J.; Imam, S.H.; Eskue, W.A.; Snell, W.J. (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". J. Cell. Biol. 108: 199–207. doi:10.1083/jcb.108.1.199. PMID 2910877.
↑ Matsuda, Y. (1998). "Gametolysin". In Barrett, A.J.; Rawlings, N.D.; Woessner, J.F. Handbook of Proteolytic Enzymes. London: Academic Press. pp. 1140–1143.
↑ Smith, Thomas; Blackman, Steve; Foster, Simon (2000). "Autolysins of Bacillus subtilis: multiple enzymes with multiple functions". Microbiology. Reading: Society for General Microbiology. 146 ( Pt 2) (146): 249–262. doi:10.1099/00221287-146-2-249. PMID 10708363. Retrieved 2007-10-07.

External links

Gametolysin at the US National Library of Medicine Medical Subject Headings (MeSH)

Proteases: metalloendopeptidases (EC 3.4.24)

ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13

Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28

Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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