Status | Page | User | Date/Time | GO Term (Aspect) | Reference | Evidence | Notes | Links |
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acceptable | 9CAUD:I1TEH9 | Eric, RedSU18 | 2018-07-14 09:16:50 CDT | GO:0008932 lytic endotransglycosylase activity (F) | PMID:24690638 | ECO:0000314 direct assay evidence used in manual assertion | Fig 4. Author analyzes endolysin target sites by isolating peptidoglycan from E. coli and treating it with SPN9CC endolysin. Different byproducts of the reactions were analyzed to determine glycosidase, amidase, and peptidase activity. Results conclusively showed that the lysin possesses glycosidase activity. Since glycosidase activity involves alteration of glycosides, it can be categorized as transglycosylase activity. The reaction product used to measure glycosidase activity was 1,6-anhydromuramic acid, which is indicative of cleavage within the peptidoglycan chain instead of cleavage at the ends. This shows that the lysin possesses endotransglycosylase activity.
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