User:Ortizla1

My Annotations

Status	Page	Date/Time	GO Term (Aspect)	Reference	Evidence	Notes	Links
acceptable	HAELO:F2Z7L0	2012-04-11 17:02:48 CDT	GO:0003796 lysozyme activity (F)	PMID:21771526	ECO:0000314 direct assay evidence used in manual assertion	Figure 4 shows the activity of recombinant HILysozyme, that was performed using Micrococcus lysodeikticus powder as a substrate. It is shown that the diameter of the clear zone depends on the protein concentration. This effect is similar to the effect caused by the egg white lysozyme used as control. (Although this data were not shown)	challenge
acceptable	ORNMO:Q95V68	2012-04-11 17:06:55 CDT	GO:0003796 lysozyme activity (F)	PMID:10560138	ECO:0000314 direct assay evidence used in manual assertion	Figure 6 shows the lytic activity of the lysozyme purified from tick gut; using a zone assay with M. luteus. Moreover, Fig. 7 displays the determination of pH optimum of the tick gut lysozyme and its comparison with egg lysozyme.	challenge
unacceptable	?	2012-04-10 20:56:58 CDT	GO:0004345 glucose-6-phosphate dehydrogenase activity (Table II shows substrate and coenzyme specificities of A. hansenii NADP-Linked G6PD. The results showed that G6PD is NADP- preferring.)	PMID:1929428	IDA: Inferred from Direct Assay		challenge
requireschanges	MOUSE:LPCT4	2012-04-10 22:31:52 CDT	GO:0003841 1-acylglycerol-3-phosphate O-acyltransferase activity (F)	PMID:19114731	ECO:0000314 direct assay evidence used in manual assertion	Figures 4 shows the Acyltransferase activity measured by the transfer of [1-14C]acyl-CoAs or [3H]acetyl-CoA to lysophospholipids to form phospholipids. The lysophospholipid preferences of mLPAAT3 were determined. The substrate specificity of the mLPAAT3 enzyme was measure using [1-14C]arachidonoyl-CoA as an acyl donor, and using a variety of lysophospholipid acceptors.	challenge
acceptable	CYNCS:D2CVT3	2012-04-11 17:33:44 CDT	GO:0004097 catechol oxidase activity (F)	PMID:15686433	ECO:0000314 direct assay evidence used in manual assertion	Table 2 shows data from the Lineweaver- Burk plot analysis of this enzyme preparation, in order to test substrate specificity. 4-methylcatechol was the most suitable substrate for this enzyme	challenge
acceptable	LEIDO:G9JM00	2012-04-11 20:28:23 CDT	GO:0004751 ribose-5-phosphate isomerase activity (F)	PMID:22483752	ECO:0000314 direct assay evidence used in manual assertion	Figure 4 shows the Lineweaver–Burk plot representation of the LdRpiB kinetics data. Recombinant Ld RpiB activity was assayed in the presence of different concentrations of ribose 5-phosphate (R5P)	challenge

acceptable:4
unacceptable:1
requires_changes:1
flagged:0

Annotations challenged by Ortizla1

Status	Author,Group	Page	GO Term (Aspect)	Reference	Evidence	Links	Page history

0 annotations fixed by Ortizla1

My Annotations

Status	Page	Date/Time	GO Term (Aspect)	Reference	Evidence	Notes	Links
acceptable	PSEAE:SPEA	2012-04-01 16:57:13 CDT	GO:0008792 arginine decarboxylase activity (F)	PMID:12634339	ECO:0000315 mutant phenotype evidence used in manual assertion	Table 2 shows the formation of arginine decarboxylase (ADC) by the wild-type strain and the speA mutants under different growth conditions. Spe A mutant had lower levels of ADC.	challenge
requireschanges	PSEAE:Q9HVQ3	2012-04-01 16:55:44 CDT	GO:0006593 ornithine catabolic process (P)	PMID:12634339	ECO:0000315 mutant phenotype evidence used in manual assertion	Table 2 shows the formation of ornithine decarboxylase (ODC) by the wild-type strain and the speC mutants under different growth conditions. Spe C mutants had lower levels of ODC.	challenge
requireschanges	PSEAE:AGUA	2012-03-31 08:38:22 CDT	GO:0047632 agmatine deiminase activity (F)	PMID:11673419	ECO:0000315 mutant phenotype evidence used in manual assertion	Figure 3 shows the expression profile of aguBA strain with different carbon and nitrogen sources. The agmatine deiminase activity (AguA) was induced in media containing agmatine. Table 2 shows these data as well; but displaying that in the mutant of the repressor operon, the enzyme was constitutively expressed.	challenge
acceptable	ECOLI:CLPX	2012-03-31 17:22:33 CDT	GO:0004176 ATP-dependent peptidase activity (F)	PMID:8226769	ECO:0000314 direct assay evidence used in manual assertion	Figure 7 and 9 show degradation of the lamba O protein by the ClpXP protease, being completely dependent on the presence of ATP, whereas table IV shows results for several nucleotides tested as energy source. The data demonstrated the ATP specificity of this protease.	challenge

acceptable:2
unacceptable:0
requires_changes:2
flagged:0

Annotations challenged by Ortizla1

Status	Author,Group	Page	GO Term (Aspect)	Reference	Evidence	Links	Page history

0 annotations fixed by Ortizla1