User:Mhassan

My Annotations

Status	Page	Date/Time	GO Term (Aspect)	Reference	Evidence	Notes	Links
unacceptable	9CAUD:S5Y0G6	2015-04-08 08:17:31 CDT	GO:0004146 dihydrofolate reductase activity (F)	GO_REF:0000100	ECO:0000247 sequence alignment evidence used in manual assertion	HHPred showed promising alignment with e value=5E-45, p value=2.6E-50, and prob =100.0. This gene is a putative homologue of the prior one as evidenced by the alignment and shared function. Primary paper supports DHFR activity by mutant phenotpe. "e KM values of NADPH and H2F for the wild type spDHFR and the mutant Sp9 were measured (Table 2B). The KM values for the wild type spDHFR were at least order of magnitude higher than those for the Sp9 mutant that showed full enzyme activity even at a limiting low concentration of 0.63 μM H2F consistent with a much lower KM value for this substrate. "	challenge
acceptable	STREE:O85255	2015-05-11 13:55:15 CDT	GO:0004146 dihydrofolate reductase activity (F)	PMID:19950924	ECO:0000315 mutant phenotype evidence used in manual assertion	Figure 8 shows how the mutation of Val100 to Leu makes the leucine side chain clash with side chains of Ile8 and Phe34, shifting their positions and stacking interactions with the trimethoprim molecule. "Weaker binding of trimethoprim to Leu100 DHFR would lead to trimethoprim resistance". The KM values of NADPH and H2F for the wild type spDHFR and the mutant Sp9 were measured (Table 2B). The KM values for the wild type spDHFR were at least order of magnitude higher than those for the Sp9 mutant that showed full enzyme activity even at a limiting low concentration of 0.63 μM H2F consistent with a much lower KM value for this substrate.	challenge

acceptable:1
unacceptable:1
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Annotations challenged by Mhassan

Status	Author,Group	Page	GO Term (Aspect)	Reference	Evidence	Links	Page history
acceptable	Hasli, TeamPurple	9CAUD:S5Y0G6	GO:0004146 - dihydrofolate reductase activity (F)	GO_REF:0000100	ECO:0000247 sequence alignment evidence used in manual assertion	challenge	C: 1

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