UMBC Phage Hunters Spring 2015
My Annotations
| Status | Page | Date/Time | GO Term (Aspect) | Reference | Evidence | Notes | Links |
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| updatedbyinstructor | 9CAUD:J9PU17 | 2015-04-07 17:29:32 CDT | GO:0008745 N-acetylmuramoyl-L-alanine amidase activity (F) | PMID:22524239 | ECO:0000314 direct assay evidence used in manual assertion | Peptidoglycan of B. cereus was incubated with 5 micrograms LysBPS13 for 30 min to determine the amidase activity of LysBPS13 by the amount of free N-acteylmuramic acid liberated. The N-acteylmuramic acid product was first degraded to lactic acid, and then acetaldehyde to be identified colorimetrically with p-hydroxydiphenyl (PHD). The results showed an increase in free N-acteylmuramic acid from cleavage of the bond between N-acetylmuramic acid and L-alanine (Figure 2), demonstrating LysBPS13 has N-acetylmuramyl-L-alanine amidase activity. A glycosidase assay ruled-out LysBPS13 as a glucosaminidase or a muramidase by showing free reducing sugars were not generated by the peptidoglycan after LysBPS13 treatment. Additionally, when 5 micrograms/milliliter of purified, recombinant LysBPS13 was added to B. cereus cells, almost all the B. cereus cells were effectively lysed within 10 min (Figure 1.c), further supporting N-acetylmuramoyl-L-alanine amidase activity of LysBPS13.
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Annotations challenged by Dnicholas
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