| Structural highlights
1h6m is a 1 chain structure with sequence from Chick. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| Related: | 1w6z, 1kxx, 4lyo, 3lyo, 1kip, 1t6v, 1ic7, 1vds, 1lzt, 1kir, 2xbr, 1lys, 1bwj, 132l, 1e8l, 1yil, 1heo, 1sfg, 1kxw, 2x0a, 2c8o, 1yl1, 1sf4, 1g7l, 1ior, 1h87, 1ljg, 3lyt, 1dpx, 1iot, 1v7s, 1ja6, 1jis, 1ir8, 2w1m, 1uic, 1xgq, 1ykz, 1uie, 2war, 1lji, 8lyz, 1lj3, 1dpw, 2lyo, 2iff, 1bwi, 1g7h, 1jj0, 1lks, 1rfp, 5lyt, 1jiy, 1sfb, 1iee, 1xei, 1ir7, 1xek, 1hel, 1at6, 1ljf, 1mlc, 1f10, 2b5z, 193l, 1lsz, 1ljk, 6lyt, 1sq2, 1vdq, 1zmy, 2d91, 1lje, 2xth, 1b2k, 1lze, 1aki, 1hen, 1uia, 1yik, 1xfp, 2d6b, 1lpi, 1ndg, 1flw, 1lsd, 2blx, 6lyz, 1nbz, 1lsg, 4lyt, 1ved, 3hfm, 1jit, 1lzn, 1lyz, 1wtn, 1ja2, 1uuz, 2xbs, 2d4i, 2fbb, 2lym, 1fdl, 1gxx, 1lz9, 1lse, 1lzh, 1lsm, 3lym, 7lyz, 1jj3, 1yky, 1t3p, 1heq, 1kiq, 2lzh, 1uih, 1kxy, 2w1l, 2bly, 1b0d, 1g7j, 1bhz, 1her, 1wtm, 1hep, 1ioq, 1nby, 1jtt, 1qio, 1lza, 1xgp, 1ps5, 1gwd, 1v7t, 1jpo, 1dqj, 2a7d, 1j1p, 2c8p, 1z55, 1ljj, 1lsb, 1f0w, 2w1x, 1lzg, 1flq, 1lzc, 1jj1, 1rcm, 1uid, 1yqv, 1hsx, 1bgi, 1lcn, 1lzd, 1hew, 2cds, 2vb1, 2aub, 1hf4, 1uib, 1ir9, 2cgi, 1j1x, 1rjc, 1ios, 1uc0, 1azf, 1ljh, 1ic4, 4lyz, 1gpq, 2a6u, 2d4k, 1xej, 1ja7, 1mel, 1ri8, 1uig, 1bvx, 1qtk, 1c10, 1lkr, 1lyo, 2xjw, 1hsw, 1n4f, 2w1y, 1jto, 1g7m, 1sf7, 1lsf, 1fn5, 5lyz, 2d4j, 1c08, 3lzt, 1ndm, 1sf6, 3lyz, 1bvk, 1uif, 2lyz, 1vau, 1fly, 1lma, 1yl0, 1j1o, 1hc0, 2lzt, 4lzt, 1a2y, 1uco, 1lsy, 1lsa, 1ic5, 1p2c, 5lym, 1gxv, 1ua6, 1at5, 1f3j, 1vat, 1lj4, 1hem, 1vfb, 1ja4, 4lym, 2a7f, 194l, 1flu, 1lz8, 1ykx, 1bwh, 2hfm, 1vdt, 1io5, 1lsn, 1lzb, 2bpu, 1g7i, 1lsc, 1vdp |
| Activity: | Lysozyme, with EC number 3.2.1.17 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Hen egg-white lysozyme (HEWL) was the first enzyme to have its three-dimensional structure determined by X-ray diffraction techniques. A catalytic mechanism, featuring a long-lived oxocarbenium-ion intermediate, was proposed on the basis of model-building studies. The 'Phillips' mechanism is widely held as the paradigm for the catalytic mechanism of beta-glycosidases that cleave glycosidic linkages with net retention of configuration of the anomeric centre. Studies with other retaining beta-glycosidases, however, provide strong evidence pointing to a common mechanism for these enzymes that involves a covalent glycosyl-enzyme intermediate, as previously postulated. Here we show, in three different cases using electrospray ionization mass spectrometry, a catalytically competent covalent glycosyl-enzyme intermediate during the catalytic cycle of HEWL. We also show the three-dimensional structure of this intermediate as determined by X-ray diffraction. We formulate a general catalytic mechanism for all retaining beta-glycosidases that includes substrate distortion, formation of a covalent intermediate, and the electrophilic migration of C1 along the reaction coordinate.
Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate.,Vocadlo DJ, Davies GJ, Laine R, Withers SG Nature. 2001 Aug 23;412(6849):835-8. PMID:11518970[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
- ↑ Vocadlo DJ, Davies GJ, Laine R, Withers SG. Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature. 2001 Aug 23;412(6849):835-8. PMID:11518970 doi:10.1038/35090602
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