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User:Ratiujer

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My Annotations

StatusPageDate/TimeGO Term (Aspect)ReferenceEvidenceNotesLinks
acceptableMYCTU:I6X5U42013-04-09 11:38:18 CDTGO:0008171 O-methyltransferase activity (F)PMID:23536839ECO:0000314 direct assay evidence used in manual assertion

Figure 4 shows that Rv2954c is responsible for the o-methylation of the hydroxyl group at position 3 of the terminal fucosyl residue of the phenolic glycolipids produced by M. tuberculosis. This conclusion is supported by the differences observed in the biochemical analyses of the glycolipid product of the Rv2954c mutant (PMM115:pPET1)compared to the same analyses of the glycolipid product of the wild-type strain. The biochemical analyses presented in figure 4 include: MALDI-TOF Mass Spec, 1D 1H-NMR, and 2D-COSY.

challenge
updatedbyinstructorMYCTU:P951372013-04-09 11:48:15 CDTGO:0008171 O-methyltransferase activity (F)PMID:23536839ECO:0000314 direct assay evidence used in manual assertion

Figure 5 shows that Rv2955c is responsible for catalyzing the o-methylation of position 4 of the fucosyl residue of the phenolic glycolipid produced by M. tuberculosis H37Rv. Figure 5 shows the results of the biochemical analyses of the glycolipid products generated in the two Rv2955c mutant strains.

challenge
acceptableBRELN:Q5MQ312013-04-09 16:47:38 CDTGO:0018826 methionine gamma-lyase activity (F)PMID:15574935ECO:0000315 mutant phenotype evidence used in manual assertion

Figure 1 shows the l-methionine-gamma-lyase knockout mutant fails to produce methanthiol, alpha-ketobutyrate, and ammonia. Figure 1 also shows the wild type strain produces large amounts of methanthiol, alpha-ketobutyrate.

challenge
acceptableMYCTU:I6Y2422013-04-11 12:18:31 CDTGO:0008171 O-methyltransferase activity (F)PMID:23536839ECO:0000314 direct assay evidence used in manual assertion

Figure 6 shows that Rv2956 is responsible for catalyzing the O-methylation of position 2 of the terminal fucosyl residue of the phenolic glycolipid produced by M. tuberculosis H37Rv. Figure 6 shows the results of the biochemical analyses of the glycolipid products of the Rv2956 mutant strain.

challenge
updatedbyinstructor9BACL:I0BWH52013-04-11 12:18:47 CDTGO:0044406 adhesion to host (P)PMID:22615573ECO:0000315 mutant phenotype evidence used in manual assertion

Figure 5 shows that in an adhesion assay the splA knockout mutant had as little as 5.36% of the adhesion capacity to larval midgut cells compared to that of the ERICII (04-309wt) wild-type allele.

challenge
updatedbyinstructorLACPA:S2QWF92013-04-11 12:54:33 CDTGO:0033938 1,6-alpha-L-fucosidase activity (F)PMID:21097595ECO:0000314 direct assay evidence used in manual assertion

Table 2 shows the data for the enzymatic activities of alfA in the presence of various natural fucosylated substrates. The enzymatic activity was determined by measuring the amount of fucose produced(umol) per milligram of enzyme per minute. The data shows that AlfA only catalyzes the hydrolysis of 6'-Fucosyl-GlcNAc.

challenge
acceptableSTRCO:Q9K3P62013-04-11 23:34:52 CDTGO:0008195 phosphatidate phosphatase activity (F)PMID:23356794ECO:0000314 direct assay evidence used in manual assertion

Figure 3 shows that heterologous expression of SCO1102 in E. coli resulted in increased amounts of fatty acid as well as diacylglycerol compared to the amounts of each produced by the control strain.

challenge
acceptablePSEAI:Q513532013-04-14 16:40:14 CDTGO:0004576 oligosaccharyl transferase activity (F)PMID:17890310ECO:0000314 direct assay evidence used in manual assertion

Figure 1a shows that the pilO knockout mutant is incapable of producing glycosylated pillin, whereas the wild-type strain did produce glycosylated pillin. Figure 1a shows the picture of the gel from western-blot analysis of whole cell extracts from both the wild-type strain and the pilO mutatnt containing unglycosylated and glycosylated pillin.

challenge

acceptable:5
unacceptable:0
requires_changes:0
flagged:0

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