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User:Adkinstr

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CACAO Spring 2014

My Annotations

StatusPageDate/TimeGO Term (Aspect)ReferenceEvidenceNotesLinks
updatedbyinstructorBACSU:PUTP2014-04-01 12:37:33 CDTGO:0015193 L-proline transmembrane transporter activity (F)PMID:22139509ECO:0000315 mutant phenotype evidence used in manual assertion

Table 3: The PutP+ strain BLOB9 exhibits high-affinity l-proline transport activity (Km, about 8 μM) with a rather modest capacity (Vmax, about 29 nmol min−1 mg protein−1) in cells that were grown in SMM. However, precultivation of this strain in SMM in the presence of 1 mM l-proline increased l-[14C]proline uptake activity by about 6-fold (Vmax, about 158 nmol min−1 mg protein−1) without influencing the substrate affinity (Km) of the PutP transport system.

challenge
requireschangesECOLI:PUTP2014-04-01 17:16:21 CDTGO:0005296 L-proline permease activity (F)PMID:24358297ECO:0000314 direct assay evidence used in manual assertion

Figure 2a: A direct assay is preformed upon the H. pylori gene, HpPutP, in E coli. The uptake of L-proline into E. coli (harboring HpPutP) was much greater than cells transformed with pT7-5, the negative control in this experiment. Without HpPutP present in the cell, L-proline cannot be transported into the cell.

challenge
acceptableMYCSM:DHA2014-04-01 18:23:27 CDTGO:0000286 alanine dehydrogenase activity (F)PMID:12193615ECO:0000315 mutant phenotype evidence used in manual assertion

Figure 4c: Displays the results from the analysis of L-alanine dehydrogenase activities in M. smegmatis wild type, mutant, and recombinant strains. The wild type strain (mc2155) with added L-alanine has the highest specific activity levels, compared to ald mutant and recombinant strains.

challenge
unacceptableMYCSM:DHA2014-04-01 18:37:59 CDTGO:0000286 alanine dehydrogenase activity (F)PMID:12193615ECO:0000315 mutant phenotype evidence used in manual assertion

Figure 6b: Shows the utilization of nitrogen sources by M. smegmatis wild-type, ald null mutant, and complemented strains. Exponentially of each strain were harvested, washed, and inoculated into minimal medium containing L-alanine as the sole nitrogen source. More viable cells were produced in the wild type strain compared to mutant and complemented strains. This is because alanine dehydrogenase catalyzes a reaction that generates nitrogen from L-alanine.

challenge
unacceptableBACIU:J7JJI72014-04-01 19:24:29 CDTGO:0051699 proline oxidase activity (Figure 2b: Results from the transcriptional analysis of putB expression by RT-PCR with putB-specific primers and 16S rRNA-specific primers. putB is expressed in the wild type, but not in the prcR mutant. Without the transcriptional activator, prcR, putB is not transcribed. This means that L-proline cannot be utilized as a nutrient source.)PMID:21964733IMP: Inferred from Mutant Phenotype
challenge
unacceptableHCMVA:GB2014-04-05 19:07:30 CDTGO:0046718 viral entry into host cell (P)PMID:24658280ECO:0000314 direct assay evidence used in manual assertion

Figure 4 shows how glycoprotein B is involved in the human cytomegalovirus entry into primary glioblastoma cells.

challenge
updatedbyinstructorBACSU:ROCA22014-04-06 10:16:43 CDTGO:0004657 proline dehydrogenase activity (F)PMID:22139509ECO:0000315 mutant phenotype evidence used in manual assertion

Evidence for proline dehydrogenase is in the text, not a figure or table "The addition of L-proline to B. subtilis cultures grown in SMM increased PRODH activity 5-fold from 0.48 ± 0.05 U (mg protein−1) to 2.69 ± 0.21 U (mg protein−1). This increase in PRODH activity was abolished in a putB mutant that possessed an activity of 0.46 ± 0.02 U (mg protein−1) in cells grown in the absence of L-proline and 0.45 ± 0.02 U (mg protein−1) in cells cultivated in the presence of L-proline."

challenge
updatedbyinstructorHUMAN:Q96QB22014-04-06 13:21:43 CDTGO:0015804 neutral amino acid transport (P)PMID:24671056ECO:0000315 mutant phenotype evidence used in manual assertion

Figure 1B shows how when JPH203, a LAT-1 specific inhibitor was used then the amount of the neutral amino acid leucine was decreased. This shows how when LAT-1 is functional LAT1 acts to support effective uptake of amino acids, which is critical for the optimal function of HUVECs for angiogenesis.

challenge

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unacceptable:3
requires_changes:1
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