Sandbox 42: Difference between revisions
From Proteopedia
Jump to navigationJump to search
mNo edit summary |
mNo edit summary |
||
| Line 1: | Line 1: | ||
<!-- PLEASE DO NOT DELETE THIS TEMPLATE --> | <!-- PLEASE DO NOT DELETE THIS TEMPLATE --> | ||
{{Template:Oberholser_Sandbox_Reservation}} | {{Template:Oberholser_Sandbox_Reservation}} | ||
| Line 6: | Line 5: | ||
== Overview == | == Overview == | ||
The primary catalytic action of the enzyme lysozyme is to hydrolyze β(1→4) glycosidic linkages found in bacterial cell walls. | The primary catalytic action of the enzyme lysozyme is to hydrolyze β(1→4) glycosidic linkages found in bacterial cell walls.<ref>http://lysozyme.co.uk/</ref> More specifically, lysozyme hydrolyzes the linkages from ''N''-acetylmuramic acid to ''N''-acetylglucosamine which occur in peptidoglycans of the cell wall. The small 14.3 kD Hen egg white lysozyme is one of the most widely studied lysozymes. | ||
== Secondary structure == | == Secondary structure == | ||
Hen egg white lysozyme is formed from one polypetide chain 129 amino acids in length. 4 disulfide bonds are involved in folding of the chain. | Hen egg white lysozyme is formed from one polypetide chain 129 amino acids in length. 4 disulfide bonds are involved in folding of the chain. | ||
| Line 15: | Line 14: | ||
== References == | == References == | ||
<references/> | |||
