Part:BBa_K2888000:Design
cyanophage lysozyme gene
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Introduction
1. The aspartic and glutamic acid residues at the active site of the lysozyme would wrap around the glycosidic bond between 6 carbon conponent N-acetylmuramic acid （NAM）and N-acetylglucosamine (NAG) of the carbohydrate section of the peptidoglycan. The carboxyl group on the aspartic acid attacks the carbon on NAM, attaching the aspartic acid to the NAM. Meanwhile, an oxygen on the NAG would pick up the hydrogen proton on the glutamic acid, deprotonating the glutamic acid into a glutamate.
2. The lysis of lysozyme has to take place in aqueous environment. The addition of a water molecule would complete the hydrolysis reaction by protonating the glutamate back to glutamic acid; it would also deprotonate the aspartic acid from the NAM, restoring it back to its reduced form, while leaving a hydroxyl group on the end of NAM. This way, the lysozyme would keep its own structure unchanged while degrading the carbohydrate section of the peptidoglycan into the NAM/NAG components.
Source
This cyanophage lysozyme is discovered by Heideburg et al in Yellowstone National Park {Heideburg:2009hb} among 29 lysozyme family.
References
Jensen HB, Kleppe K: Effect of ionic strength, pH, amines and divalent cations on the lytic activity of T4 lysozyme. Eur J Biochem 1972, 28:116–122.
Kunal Mehta, Niklaus Evitt, James Swartz: Chemical Lysis of Cyanobacteria. Journal of Biological Engineer, 9/10/2015