Lysozyme, also known as muramidase or N-acetylmuramide glycanhydrolase, are

glycoside hydrolases, enzymes (EC 3.2.1.17) that damage bacterial cell walls by
catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-
acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-
glucosamine residues in chitodextrins. Lysozyme is abundant in a number of
secretions, such as tears, saliva, human milk, and mucus. It is also present in
cytoplasmic granules of the polymorphonuclear neutrophils (PMN). Large amounts of
lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-
lactalbumin in sequence and structure, making them part of the same family.

In humans, the lysozyme enzyme is encoded by the LYZ gene.[1][2]

Contents
[hide]

• 1 Function
• 2 Role in disease
• 3 History
• 4 See also
• 5 References

• 6 External links

[edit] Function
The enzyme functions by attacking peptidoglycans (found in the cell walls of bacteria,
especially Gram-positive bacteria) and hydrolyzing the glycosidic bond that connects
N-acetylmuramic acid with the fourth carbon atom of N-acetylglucosamine. It does
this by binding to the peptidoglycan molecule in the binding site within the prominent
cleft between its two domains. This causes the substrate molecule to adopt a strained
conformation similar to that of the transition state[citation needed]. According to Phillips-
Mechanism, the lysozyme binds to a hexasaccharide. The lysozyme then distorts the
fourth sugar in hexasaccharide (the D ring) into a half-chair conformation. In this
stressed state, the glycosidic bond is easily broken.

The amino acid side-chains glutamic acid 35 (Glu35) and aspartate 52 (Asp52) have
been found to be critical to the activity of this enzyme. Glu35 acts as a proton donor
to the glycosidic bond, cleaving the C-O bond in the substrate, whereas Asp52 acts as
a nucleophile to generate a glycosyl enzyme intermediate. The glycosyl enzyme
intermediate then reacts with a water molecule, to give the product of hydrolysis and
leaving the enzyme unchanged.

Further information: glycoside hydrolase

[edit] Role in disease

Lysozyme is part of the innate immune system. Reduced lysozyme levels have been
associated with bronchopulmonary dysplasia in newborns.[3] Children fed infant
formula lacking lysozyme in their diet have three times the rate of diarrheal disease.[4]
Since lysozyme is a natural form of protection from pathogens like Salmonella,
E.coli, and Pseudomonas, a deficiency due to infant formula feeding can lead to
increased incidence of disease.[citation needed]

Whereas the skin is a protective barrier due to its dryness and acidity, the conjunctiva
(membrane covering the eye) is, instead, protected by secreted enzymes, mainly
lysozyme and defensin. However, when these protective barriers fail, conjunctivitis
results

[edit] History
The antibacterial property of hen egg white, due to the lysozyme it contains, was first
observed by Laschtschenko in 1909,[5] although it was not until 1922 that the name
'lysozyme' was coined, by Alexander Fleming (1881–1955), the discoverer of
penicillin.[6] Fleming first observed the antibacterial action of lysozyme when he
treated bacterial cultures with nasal mucus from a patient suffering from a head cold.
[6]

The three-dimensional structure of hen egg white lysozyme was described by David
Chilton Phillips (1924–1999) in 1965, when he obtained the first 2-Ångström (200
pm) resolution model via X-ray crystallography.[7][8] The structure was publicly
presented at a Royal Institution lecture in 1965.[9] 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.[10] 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.[11] 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.[12]

Howard Florey (1898–1968) and Ernst B. Chain (1906–1979) also investigated

lysozymes. Although they never made much progress in this field, they, along with
Fleming, developed penicillin.

http://en.wikipedia.org/wiki/Lysozyme