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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
biotransformation experiments with resting cells of Escherichia coli JM109 harboring recombinant ahd genes reveal that AhdA2cA1c, AhdA1dA2d, and AhdA1eA2e can function as a salicylate 1-hydroxylase
gene shy1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative RT-PCR enzyme expression analysis
gene shyA or NRRL3_9723, DNA and amino acid sequence determination and analysis, enzyme expression analysis, gene NRRL3_9723 shows high amino acid similarity to Shy1 from Fusarium graminearum (FgShy1) (65.1%) and to a putative salicylate hydroxylase (AN2114) from Aspergillus nidulans (77.3%), sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene shyC, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative RT-PCR enzyme expression analysis
gene Solyc08g063130, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, transient recombinant expression in Nicotiana benthamiana leaves
transgenic Populus tremula x Populus alba hybrid expressing the nahG transgene. Expression of nahG decreases quinic acid conjugates and increased catechol glucoside, while exerting little effect on levels of salicylic acid and catechol, the substrate and product, respectively, of the nahG enzyme