User:Mart1123

My Annotations

Status	Page	Date/Time	GO Term (Aspect)	Reference	Evidence	Notes	Links
acceptable	RHOMR:O33897	2012-04-12 11:37:59 CDT	GO:0008810 cellulase activity (F)	PMID:9581291	ECO:0000314 direct assay evidence used in manual assertion	Figures 2,3, and 4 show SDS page gels for the native CelA enzyme, the recombinant form of the enzyme, and a gel comparing the activity and protein of both. Figure 2 shows the native CelA molecular mass corresponds to the expected value. This information is important for future comparisons to recombinant types. Figure 3 shows the recombinant CelA molecular mass and activity after boiling with proteinase K. The control (lane 2) showed activity bands at higher molecular weights than the native enzyme. After boiling, activity began to disappear and a protein band of 26 kDa appeared in lanes 3, 4, and 5. Figure 4 shows an SDS gel with CMC for both enzymes. The native activity band appeared in a corresponding position to the smallest activity band of the recombinant enzyme. The same activity bands were seen regardless of heating with protease.	challenge
requireschanges	RHOMR:Q66SU9	2012-04-12 12:02:06 CDT	GO:0008843 endochitinase activity (F)	PMID:15583965	ECO:0000314 direct assay evidence used in manual assertion	Figure 6 shows changes in viscosity from the DDA 73% chitosan. This clearly indicates that hydrolysis occurred inside the polymers, proving that Chi is an endoacting chitinase on chitopolysaccharides.	challenge
acceptable	RHOMR:MGS	2012-04-12 19:47:35 CDT	GO:0051479 mannosylglycerate biosynthetic process (P)	PMID:10585410	ECO:0000314 direct assay evidence used in manual assertion	Table 2 shows the activity of the native and recombinant enzymes and their ability to utilize substrates in the mannosylglycerate biosynthetic pathway. The native enzyme was obtained by electroelution and had a specific activity of 70mmol/min/mg of protein. The substrates used to determine the specificity of Mgs were GDP mannose, ADP mannose, UDP mannose,mannose 1-phosphate, and mannose 6-phosphate as sugar donors,and D-glycerate,L-glycerate, and D-3-P-glycerate as sugar acceptors. GDP glucose, UDP glucose, and ADP glucose were tested as sugar donors, and glycerol 3-phosphate, glucose 6-phosphate,glucose 1-phosphate, and glucose as sugar acceptors in an effort to also identify the ability of Mgs to catalyze the synthesis of other glycosylconjugates. Mgs was specific for GDP mannose and D-glycerate and had an absolute stereospecificity for D-glycerate. UDP mannose and GDP mannose were the only sugar nucleotides used by the enzyme. UDP mannose was used very little, less than 3% of that of GDP mannose. NaCl and KCl (50-500 mM concentrations) had no effect on enzyme activity. However, Mg2+ was required for optimal activity shown by the 2.5-fold lower activity in absence of the cation.	challenge
requireschanges	RHOMR:O52754	2012-04-12 18:25:31 CDT	GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds (F)	PMID:9799108	ECO:0000314 direct assay evidence used in manual assertion	Figures 5 and 6 confirm the hydrolase function of the LamR enzyme, which is expressed by the lamR gene. Both figures show digests separated by TLC. In figure 5, the intermediate appearance of oligosaccharides detected after a short incubation time prove that the hydrolysis of 1,3-1,4-beta-glucan and laminarin follows the endo type action pattern. In figure 6, LamR displayed a weak and significant activity against cellobiosyl-glucose G1-4G1-3Gr, which suggests that LamR is able to cut specific beta linkages only in low-molecular-mass carbohydrates.	challenge
acceptable	BUTFI:GLGB	2012-04-15 13:14:01 CDT	GO:0003844 1,4-alpha-glucan branching enzyme activity (F)	PMID:1938880	ECO:0000314 direct assay evidence used in manual assertion	Figure 9 shows the absorbance spectra of the iodine-glucan complex of the a-glucan formed de novo by the purified branching enzyme and phosphorylase a (ratio of 1:1). The combination of the actions of phosphorylase a and GlgB yielded a branched product with a spectrum similar to glycogen. The initial Xmax was 490nm, but as the reaction proceeded decreased to 430nm, indicating a highly branched product.	challenge

acceptable:3
unacceptable:0
requires_changes:2
flagged:0

Annotations challenged by Mart1123

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

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My Annotations

Status	Page	Date/Time	GO Term (Aspect)	Reference	Evidence	Notes	Links
requireschanges	STRPN:A7KT31	2012-03-29 12:38:22 CDT	GO:0086080 protein binding involved in heterotypic cell-cell adhesion (F)	PMID:17850254	ECO:0000315 mutant phenotype evidence used in manual assertion	Figure 5 RrgA is involved in pilus-mediated colonization of the upper respiratory tract in mice. The mice were infected with T4 phage with rrgA and rrgB/rrgC deletions respectively. Seven days after infection, Mice infected with T4 rrgA deletion phage had significantly less bacteria in the nasopharynx than mice infected with T4 rrgB/rrgC deletion phage. This demonstrates that rrgA is important for pilli assembly and strong cell wall adhesion.	challenge

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

Annotations challenged by Mart1123

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

0 annotations fixed by Mart1123