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Results 1 - 8 of 8
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a heterologous system is constructed in which the C domain of EiAPR was fused to the carboxyl terminus of the APS reductase from Pseudomonas aeruginosa (PaAPR), an enzyme that normally uses thioredoxin as an electron donor and is incapable of using glutathione for this function. The hybrid enzyme, which retains the [4Fe-4S] cluster from PaAPR can use both thioredoxin and glutathione as an electron donor for 5'-adenylylsulfate reduction. Expression in Escherichia coli
APR, DNA and amino acid sequence determination and analysis, semiquantitative expression analysis, overexpression of His-tagged APR isozyme in Escherichia coli
expressed in Escherichia coli strain BL21(DE3)-pLysS
expression in Escherichia coli
expression of N-terminally His-tagged PpAPR in Escherichia coli, expression of GFP-tagged APR in Physcomitrella patens plants using the mAV4 vector containing the chloroplast transit peptide from Physcomitrella patens FtsZ2-1 and transient transfection of protoplasts; overexpression in Escherichia coli
gene APR1, expression of the holoenzyme APR1p in Escherichia coli strain BL21(DE3), separate expression in Escherichia coli strain BL21(DE3) of amino acid residues 73-327, forming the R-domain, and of residues 328-465, forming the C-domain, the domains alone are inactive, but mixing of both can partially restore activity
recombinant expression of the enzyme, fused to the transit peptide rbcS, in Arabidopsis thaliana under transcriptional control of the CaMV 35S promotor
Results 1 - 8 of 8