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Category:MichSt14A 34

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StatusPageUserDate/TimeGO Term (Aspect)ReferenceEvidenceNotesLinks
unacceptableECOLI:OMPFGilbe205, MichSt14A 342014-04-06 15:45:02 CDTGO:0015288 porin activity (F)PMID:8702816ECO:0000315 mutant phenotype evidence used in manual assertion

Figure 3 shows the differing growth rate of wild-type and OmpF mutants when grown on maltotriose and maltooligosaccharides. The N-terminal mutations allow for growth on carbon sources larger than the normal exclusion limit.

challenge
acceptableHUMAN:INO1Gilbe205, MichSt14A 342014-04-06 14:23:22 CDTGO:0004512 inositol-3-phosphate synthase activity (F)PMID:23902760ECO:0000315 mutant phenotype evidence used in manual assertion

Figure 8C shows the effect of point mutations on the activity of the inositol-3-phosphate synthase. The assay measured the inorganic phosphate liberated from glucose 6-phosphate which is dependent on the activity of the synthase enzyme.

challenge
unacceptableECOLI:GLGBGilbe205, MichSt14A 342014-04-06 12:57:04 CDTGO:0004373 glycogen (starch) synthase activity (F)PMID:19244233ECO:0000266 sequence orthology evidence used in manual assertion

Table 2 presents the partial alignment of conserved residues between Escherichia coli glycogen synthase and other bacterial glycogen syntheses and plant starch syntheses.

challenge
unacceptableECOLI:GLGBGilbe205, MichSt14A 342014-04-06 12:32:45 CDTGO:0003844 1,4-alpha-glucan branching enzyme activity (F)PMID:12196524ECO:0000315 mutant phenotype evidence used in manual assertion

Table 5 shows sequence point mutations, deletions or truncations that result in glycogen storage disease type IV, caused by lethal or retarded function of glycogen branching enzyme.

challenge
unacceptableBOMMO:H9JTG9Gilbe205, MichSt14A 342014-04-06 12:13:51 CDTGO:0004033 aldo-keto reductase (NADP) activity (F)PMID:24012638ECO:0000266 sequence orthology evidence used in manual assertion

Figure 2 shows sequence and structural homology to other defined aldo-keto reductases, notably human aldo-keto reductase AKR1C2.

challenge

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