Editing Lysozyme (section)

== History ==

The antibacterial property of hen egg white, due to the lysozyme it contains, was first observed by Laschtschenko in 1909.<ref name = "Laschtschenko">{{cite journal | vauthors = Laschtschenko P | title = Über die keimtötende und entwicklungshemmende Wirkung Hühnereiweiß |trans-title=On the germ-killing and growth-inhibiting effect of chicken egg albumin | journal = Zeitschrift für Hygiene und Infektionskrankheiten | year = 1909 | volume = 64  | pages = 419–427 | language = de | doi = 10.1007/BF02216170| s2cid = 456259 }}</ref> The bacteria-killing activity of nasal mucus was demonstrated in 1922 by [[Alexander Fleming]], the discoverer of [[penicillin]], who coined the term "lysozyme".<ref>{{cite journal | vauthors = Duckett S | title = Ernest Duchesne and the concept of fungal antibiotic therapy | journal = Lancet | volume = 354 | issue = 9195 | pages = 2068–2071 | date = December 1999 | pmid = 10636385 | doi = 10.1016/S0140-6736(99)03162-1 | s2cid = 206011471 }}</ref> He is reported as saying: "As this substance has properties akin to those of ferments I have called it a 'Lysozyme'."<ref name="Fleming_1922">{{cite journal | vauthors = Fleming A | title = On a remarkable bacteriolytic element found in tissues and secretions  |  journal = [[Proceedings of the Royal Society B]] | volume = 93 | issue = 653 | pages = 306–317 | date = May 1922 | doi = 10.1098/rspb.1922.0023 | jstor=80959| bibcode = 1922RSPSB..93..306F | doi-access = free }}</ref> Fleming went on to show that an enzymic substance was present in a wide variety of secretions and was capable of rapidly lysing (i.e. dissolving) different bacteria, particularly a yellow "coccus"<!--italics?--> that he studied".<ref>{{cite book|title=Advances in Protein Chemistry|url=https://books.google.com/books?id=U1P3a5hjbSAC&pg=PA176|date=13 June 1991|publisher=Academic Press|isbn=978-0-08-058214-6|pages=176–}}</ref>

Lysozyme was first crystallised by [[Edward Abraham]] in 1937, enabling the three-dimensional structure of hen egg white lysozyme to be described by [[David Chilton Phillips]] in 1965, when he obtained the first 2-[[ångström]] (200 [[picometer|pm]]) resolution model via [[X-ray crystallography]].<ref>{{cite journal | vauthors = Blake CC, Koenig DF, Mair GA, North AC, Phillips DC, Sarma VR | title = Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution | journal = Nature | volume = 206 | issue = 4986 | pages = 757–761 | date = May 1965 | pmid = 5891407 | doi = 10.1038/206757a0 | s2cid = 4161467 }}</ref><ref>{{cite journal | vauthors = Johnson LN, Phillips DC | title = Structure of some crystalline lysozyme-inhibitor complexes determined by X-ray analysis at 6 Angstrom resolution | journal = Nature | volume = 206 | issue = 4986 | pages = 761–763 | date = May 1965 | pmid = 5840126 | doi = 10.1038/206761a0 | s2cid = 10234792 }}</ref> The structure was publicly presented at a [[Royal Institution]] lecture in 1965.<ref name="Johnson1998">{{cite journal | vauthors = Johnson LN | title = The early history of lysozyme | journal = Nature Structural Biology | volume = 5 | issue = 11 | pages = 942–944 | date = November 1998 | pmid = 9808036 | doi = 10.1038/2917 | s2cid = 2629199 }}</ref>
Lysozyme was the second protein structure and the first enzyme structure to be solved via X-ray diffraction methods, and the first enzyme to be fully sequenced that contains all twenty common amino acids.<ref name="Canfield1963">{{cite journal | vauthors = Canfield RE | title = The Amino Acid Sequence of Egg White Lysozyme | journal = The Journal of Biological Chemistry | volume = 238 | issue = 8 | pages = 2698–2707 | date = August 1963 | pmid = 14063294 | doi = 10.1016/S0021-9258(18)67888-3 | doi-access = free }}</ref>
As a result of Phillips' elucidation of the structure of lysozyme, it was also the first enzyme to have a detailed, specific mechanism suggested for its method of catalytic action.<ref>{{cite journal | vauthors = Vernon CA | title = The mechanisms of hydrolysis of glycosides and their revelance [sic] to enzyme-catalysed reactions | journal = Proceedings of the Royal Society of London. Series B, Biological Sciences | volume = 167 | issue = 1009 | pages = 389–401 | date = April 1967 | pmid = 4382802 | doi = 10.1098/rspb.1967.0036 | s2cid = 12870128 | bibcode = 1967RSPSB.167..389V | jstor = 75680 }}</ref><ref>{{cite journal | vauthors = Rupley JA | title = The binding and cleavage by lysozyme of N-acetylglucosamine oligosaccharides | journal = Proceedings of the Royal Society of London. Series B, Biological Sciences | volume = 167 | issue = 1009 | pages = 416–428 | date = April 1967 | pmid = 4382804 | doi = 10.1098/rspb.1967.0038 | s2cid = 33906706 | bibcode = 1967RSPSB.167..416R | jstor = 75682 }}</ref><ref>{{cite journal | vauthors = Sharon N | title = The chemical structure of lysozyme substrates and their cleavage by the enzyme | journal = Proceedings of the Royal Society of London. Series B, Biological Sciences | volume = 167 | issue = 1009 | pages = 402–415 | date = April 1967 | pmid = 4382803 | doi = 10.1098/rspb.1967.0037 | s2cid = 31794497 | bibcode = 1967RSPSB.167..402S | jstor = 75681 }}</ref> This work led Phillips to provide an explanation for how [[enzymes]] speed up a chemical reaction in terms of its physical structures. The original mechanism proposed by Phillips was more recently revised.<ref name="Vocadlo_2001"/>