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User:Chaudrye

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Phage Hunters Spring 2017

My Annotations

StatusPageDate/TimeGO Term (Aspect)ReferenceEvidenceNotesLinks
requireschangesSTRGL:LYSM12017-04-30 18:48:31 CDTGO:0003796 lysozyme activity (F)PMID:11427528ECO:0000314 direct assay evidence used in manual assertion

Figure 1 displays that unlike other lysozymes (HEWL, GEWL, and T4L-types), the Ch-type lysozymes have both Beta-1,4-N-acetyl- and Beta-1,4,-N,6-O-diacetylmuramidase activities. Due to this characteristic they are able to cleave the 6-O-acetylated peptidoglycans. This icnludes the peptiodglycans that are present in cell walls of Staphylococcus aureus.

Figure 2 displays that the structure of Cellosyl contributes to its function. Figure two shows that Cellosyl comprises a single domain. The enzyme is shown to have a beta/alpha-barrel fold. This is different than many other enzymes which have (Beta/alpha)8-barrels. All of these specific folds allow for the active site to be locate at the C-terminal end of the beta-barrel. Figure 3 compares the amino acid sequence of various Ch-type lysozymes and it supports that the active site is located at the C-terminal end of the Beta-barrel. It does so because it shows that the amino acids at the C-terminal ends of Beta1 and Beta4 are highly conserved among lysozymes from bacteria and Chalaropsis. Figure 4 displays how the charges are distributed on the surface of Cellosyl and how that impacts it's lysozyme activity. Due to the grove in the substrate-binding site, there is a high negative electrostatic potential. This is developed to the deep hole.

challenge
unacceptableBACAN:Q81YZ22017-04-30 19:12:06 CDTGO:0003796 lysozyme activity (F)PMID:21816821ECO:0000314 direct assay evidence used in manual assertion

Figure 1 displays that the two glycan chains are cross-peptide linked. The bond formed is what the amidase lysins target . It displays the cleavage positions of other common lysins in comparison to this lysin. Through this figure one can see that the gram-positive bacteria displays species as well as strain specific "secondary cell wall polymers" (SCWPS). These insert themselves into the lipid bilayer, which changes the appearance and the charge of the outer envelope.

Figure 2 was used in order to compare this lysin to two homologous amidase lysins to see the similar structures and distinct behaviours between them (PlyL and XlyA). Due to the high structural similarity, a test was conducted to see whether the innate catalytic acitivty of XlyA was similar to that of PlyL. Figure 3 displays that XlyA:plyL chimera failed to lyse B. subtilis, however it did lyse B. cereus.

challenge

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