Phage Hunters Spring 2017
My Annotations
| Status | Page | Date/Time | GO Term (Aspect) | Reference | Evidence | Notes | Links |
|---|
| LACCA:A0A0E2LWA2 | 2017-04-15 15:11:10 CDT | GO:0004175 endopeptidase activity (F) | PMID:23733182 | ECO:0000314 direct assay evidence used in manual assertion | fig. 3B and Table 3 show the hydrolytic specificity of the recombinant pure Lc-Lys-2 on Lactobacillus casei-purified Peptidoglycan (PG). The PG fragment obtained by digestion with Lc-Lys-2 was separated by RP-HPLC and analyzed by MALDI-TOF mass spectrometry. The HPLC profile reveal the hydrolytic specificities for Lc-Lys-2.
MS analysis of the major peaks and comparison of the obtained masses with the reference L. casei PG structure enabled identification of peptides generated by Lc-Lys-2 (Table 3) and to deduce the cleavage specificity (Fig. 3D). Lc-Lys-2 has a gamma-D-glutamyl-L-lysyl endopeptidase specificity.
| challenge |
| LACCA:K0N732 | 2017-04-15 15:30:46 CDT | GO:0008745 N-acetylmuramoyl-L-alanine amidase activity (F) | PMID:23733182 | ECO:0000314 direct assay evidence used in manual assertion | Fig. 3B and Table 3 show the hydrolytic specificity of recombinant pure Lc-Lys
on L. casei-purified Peptidoglycan (PG).
The PG fragments obtained by digestion with Lc-Lys
was separated by RP-HPLC and analyzed by MALDI-TOF mass spectrometry.
the HPLC profile reveal the hydrolytic specificities for Lc-Lys.
MS analysis of the major peaks and comparison of the obtained masses
with the reference L. casei PG structure
enabled identification of peptides generated by Lc-Lys (Table 3)
and to deduce the cleavage specificity (Fig. 3D).
Lc-Lys has an N-acetylmuramoyl-L-alanine amidase specificity,
| challenge |
| LACCA:K0N3B2 | 2017-04-15 15:36:27 CDT | GO:0004175 endopeptidase activity (F) | PMID:23733182 | ECO:0000314 direct assay evidence used in manual assertion | Fig. 3B and Table 3 show the hydrolytic specificity of recombinant pure Lc-Lys-2
on L. casei-purified Peptidoglycan (PG).
The PG fragments obtained by digestion with Lc-Lys-2
was separated by RP-HPLC and analyzed by MALDI-TOF mass spectrometry.
The HPLC profile reveal the hydrolytic specificities for Lc-Lys-2.
MS analysis of the major peaks and comparison of the obtained masses
with the reference L. casei PG structure
enabled identification of peptides generated by Lc-Lys-2 (Table 3)
and to deduce the cleavage specificity (Fig. 3D).
Lc-Lys-2 has a gamma-D-glutamyl-L-lysyl endopeptidase specificity.
| challenge |
| LACCD:A0A158SHI5 | 2017-04-15 15:44:09 CDT | GO:0008745 N-acetylmuramoyl-L-alanine amidase activity (F) | PMID:23733182 | ECO:0000314 direct assay evidence used in manual assertion | Fig. 3B and Table 3 show the hydrolytic specificity of recombinant pure Lc-Lys
on L. casei-purified Peptidoglycan (PG).
The PG fragments obtained by digestion with Lc-Lys
was separated by RP-HPLC and analyzed by MALDI-TOF mass spectrometry.
the HPLC profile reveal the hydrolytic specificities for Lc-Lys.
MS analysis of the major peaks and comparison of the obtained masses
with the reference L. casei PG structure
enabled identification of peptides generated by Lc-Lys (Table 3)
and to deduce the cleavage specificity (Fig. 3D).
Lc-Lys has an N-acetylmuramoyl-L-alanine amidase specificity,
| challenge |
| LACCD:A0A125U8R1 | 2017-04-15 15:48:32 CDT | GO:0004175 endopeptidase activity (F) | PMID:23733182 | ECO:0000314 direct assay evidence used in manual assertion | Fig. 3B and Table 3 show the hydrolytic specificity of recombinant pure Lc-Lys-2
on L. casei-purified Peptidoglycan (PG).
The PG fragments obtained by digestion with Lc-Lys-2
was separated by RP-HPLC and analyzed by MALDI-TOF mass spectrometry.
The HPLC profile reveal the hydrolytic specificities for Lc-Lys-2.
MS analysis of the major peaks and comparison of the obtained masses
with the reference L. casei PG structure
enabled identification of peptides generated by Lc-Lys-2 (Table 3)
and to deduce the cleavage specificity (Fig. 3D).
Lc-Lys-2 has a gamma-D-glutamyl-L-lysyl endopeptidase specificity.
| challenge |
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