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8 results for “Polyphenol oxidase”
Fig. 5 in L-DOPA synthesis in Mucuna pruriens (L.) DC. is regulated by polyphenol oxidase and not CYP 450/tyrosine hydroxylase: An analysis of metabolic pathway using biochemical and molecular markers
Fig. 5. The amplicons generated using degenerate primer approach. (a) Lane M-DNA ladder, Lane 1–250 bp amplicon generated using MTH –F and MTH-R primer pairs of TH gene (b) Lane M-DNA ladder, Lane 1 and 2–800 bp amplicon using primers deduced from the peptide sequence derived through LCMS/MS.
Fig. 4 in L-DOPA synthesis in Mucuna pruriens (L.) DC. is regulated by polyphenol oxidase and not CYP 450/tyrosine hydroxylase: An analysis of metabolic pathway using biochemical and molecular markers
Fig. 4. Effect of enzyme inhibitors on L-DOPA production in callus cultures of M. pruriens was estimated using HPTLC. The culture without inhibitor was treated as negative control and cultures with different concentration of the inhibitor were the test samples. (Control-untreated, C = Cimetidine at 1.98 μM and 19.8 μM; Q = Quinidine at 1.46 μM and 14.6 μM; A = L-ascorbic acid at 567 μM and 851 μM; K = Kojic acid at 703 μM and 1055 μM).
Fig. 3 in L-DOPA synthesis in Mucuna pruriens (L.) DC. is regulated by polyphenol oxidase and not CYP 450/tyrosine hydroxylase: An analysis of metabolic pathway using biochemical and molecular markers
Fig. 3. Effect of substrate concentration on partially purified enzymes. The assay was performed for PPO activity with 50 mM catechol as substrate at pH 6.0 while keeping the temperature for reaction at 30 ◦ C. For TH activity, 30 mM L-tyrosine was the substrate and assay done at pH 7.0 and 25 ◦ C.
Fig. 2 in L-DOPA synthesis in Mucuna pruriens (L.) DC. is regulated by polyphenol oxidase and not CYP 450/tyrosine hydroxylase: An analysis of metabolic pathway using biochemical and molecular markers
Fig. 2. Effect of pH on the activity of partially purified enzymes from Mucuna pruriens. The assay was performed using 50 mM catechol and 30 mM L-tyrosine as substrates for the PPO and TH enzyme activity, respectively. Four different buffers with their optimal buffering capacity in the pH range of 3–10 were used in separate assays.
Fig. 7 in L-DOPA synthesis in Mucuna pruriens (L.) DC. is regulated by polyphenol oxidase and not CYP 450/tyrosine hydroxylase: An analysis of metabolic pathway using biochemical and molecular markers
Fig. 7. Homology modelling and secondary structure prediction of PPO enzyme from Mucuna pruriens (a) Predicted secondary structure of PPO (b) Phyre2 protein model for PPO with 3D model dimensions (in Å) (X:49.941 Y:64.463 Z:57.979). Image colored by rainbow N → C terminus (c) Three dimensional SWISS protein model for PPO enzyme with two active copper binding ligands (copper ions bridging oxygen moiety is illustrated as small yellow spheres highlighted in the box), conserved histidine residues and metal complex interactions (in dotted lines). Chain A for Ligand 1: H.183, H.204, H.213, F.367, H.371; metal interactions: A:H.183, A:H.204, A:H.213. Chain A for Ligand 2: H.337, H.341, F.367, H.370, H.371; metal interactions: A:H.337, A:H.341, A:H.371). (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Fig. 6. The 1800 in L-DOPA synthesis in Mucuna pruriens (L.) DC. is regulated by polyphenol oxidase and not CYP 450/tyrosine hydroxylase: An analysis of metabolic pathway using biochemical and molecular markers
Fig. 6. The 1800 bp amplicon of full-length PPO cDNA obtained after deducing the 5′and 3′ ends through RACE analysis. Lane 1- 1 Kb DNA marker, Lane 2 and 3 the amplicon in duplicate after amplification using gene specific primers.
Fig. 1 in Recent advances in polyphenol oxidase-mediated plant stress responses
Fig. 1. Schematic diagram of plant polyphenol oxidase (PPO) gene and the mechanism for gene expression regulation. (a) The conserved PPO gene family domains. Neighbouring untranslated region (UTR, indicate in white), typical coding regions (orange) of PPO containing an N-terminal transit peptide (cTP, indicated in green), a dicopper centre CuA and CuB (blue) and the C-terminal domains (DWL motif and KFDV motif, shown in red). (b) Several players involved in the regulatory mechanism that controls PPO action upon stress, including elements of the promoter, transcription factor and microRNAs (miRs), were recently identified in a series of plants species. The MnMYB3R, miR528, miR1444, miR12112 and miR058 come from mulberry, banana, Populus trichocarpa, Salvia miltiorrhiza and grapevine, respectively. Rectangles denote the PPO gene and mRNA sequences. The ellipse represents the gibberellic acid (GA) response element (GARE) residing in the promoter region in pineapple, solid red circles represent GA, the dotted red curve shows that GA induced promoter activity through GARE by an as yet unknown mechanism. The hexagon represents the MYB-binding cis-element MSA, the black solid circle represents the transcription factor mulberry MnMYB3R. The triangle shows target sites of miR528 at the 5′-UTR of banana PPOs. The arrows indicate activation; the bars indicate inhibition. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Fig. 1 in L-DOPA synthesis in Mucuna pruriens (L.) DC. is regulated by polyphenol oxidase and not CYP 450/tyrosine hydroxylase: An analysis of metabolic pathway using biochemical and molecular markers
Fig. 1. The proposed hypothetical pathway for catecholamine biosynthesis in Mucuna pruriens.
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