Phage Hunters Spring 2016
My Annotations
| Status | Page | Date/Time | GO Term (Aspect) | Reference | Evidence | Notes | Links |
|---|
| unacceptable | GEOSE:A0A087LEM1 | 2016-05-02 10:17:12 CDT | GO:0004146 dihydrofolate reductase activity (F) | PMID:16114879 | ECO:0000314 direct assay evidence used in manual assertion | The three-dimensional structure of the dihydrofoate reductase (via X-ray crystallography) in Bacillus Stearothermophilus is iterated by Figure 3. This structure of Bacillus Stearothermophilus DHFR is the first monomeric DHFR structure from a thermophilic organism; there is also comparison between E. coli and T. maritima enzymes. IDA was used because this was the actual determination of the structure; the comparison to the other 2 enzymes helps support the functional conservation.
| challenge |
| updatedbyinstructor | GEOSE:A0A087LEM1 | 2016-05-02 10:28:36 CDT | GO:0004146 dihydrofolate reductase activity (F) | PMID:16114879 | ECO:0000315 mutant phenotype evidence used in manual assertion | Figure 4 shows BsDHFR activity as a function of reaction conditions through its pH dependence within MTEN buffer at different pH values and 40 °C with the rest at standard conditions. Optimum temperature for neutral pH of 7 was 75*C although enzyme stability was seen at pH 6.8 as a function of temperature due to very rapid loss of activity in the absence of substrate above 64 °C. pKa under standard assay was 7.5. The formation of THF is shown to be sensitive to pH since as pH increases, activity declines.
| challenge |
| unacceptable | COXBU:Q83AB2 | 2016-05-01 14:23:48 CDT | GO:0004146 dihydrofolate reductase activity (F) | GO_REF:0000100 | ECO:0000247 sequence alignment evidence used in manual assertion | Blastp results showed the dihydrofolate reductase activity relating Bacillus phage Coxiella burnetii and Bacillus Stearothermophilus with 100% identity, 100% query cover, and an e-value of 6.4E-38
| challenge |
| unacceptable | ENTFA:Q834R2 | 2016-05-01 14:25:03 CDT | GO:0004146 dihydrofolate reductase activity (F) | GO_REF:0000100 | ECO:0000247 sequence alignment evidence used in manual assertion | Blastp results showed the dihydrofolate reductase activity relating Enterococcus faecalis and Bacillus Stearothermophilus with 100% identity, 100% query cover, and an e-value of 7.2E-39
| challenge |
| unacceptable | BACAN:Q81R22 | 2016-05-01 14:27:50 CDT | GO:0004146 dihydrofolate reductase activity (F) | GO_REF:0000100 | ECO:0000247 sequence alignment evidence used in manual assertion | Blastp results showed the dihydrofolate reductase activity relating Bacillus anthracis and Bacillus Stearothermophilus with 100% identity, 100% query cover, and an e-value of 3.7E-37
| challenge |
| unacceptable | DICDI:NDKC | 2016-05-01 15:09:56 CDT | GO:0016301 kinase activity (F) | PMID:2161830 | ECO:0000314 direct assay evidence used in manual assertion | Fig.5B shows the presence of NDP kinase activity as followed by the formation of ADP resulting from phosphate transfer from ATP to dTDP. Also, in order to confirm that the enhanced NDP kinase activity measured in the extracts of bacteria transformed with pNDK was actually due to the protein encoded by the Gipl7 cDNA, Fig. 6A shows the enzime was partially purified and compared to its elution profile with that of the control extracts in Fig. 6B.
| challenge |
acceptable:0
unacceptable:5
requires_changes:0
flagged:0
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