Peroxidases (POD) and polyphenol oxidase (PPO) are enzymes that are well\r\nknown to be involved in the enzymatic browning reaction of fruits and vegetables with\r\ndifferent catalytic mechanisms. Both enzymes have some common substrates, but each also\r\nhas its specific substrates. In our computational study, the amino acid sequence of grape\r\nperoxidase (ABX) was used for the construction of models employing homology modeling\r\nmethod based on the X-ray structure of cytosolic ascorbate peroxidase from pea (PDB\r\nID:1APX), whereas the model of grape polyphenol oxidase was obtained directly from the\r\navailable X-ray structure (PDB ID:2P3X). Molecular docking of common substrates of\r\nthese two enzymes was subsequently studied. It was found that epicatechin and catechin\r\nexhibited high affinity with both enzymes, even though POD and PPO have different\r\nbinding pockets regarding the size and the key amino acids involved in binding. Predicted\r\nbinding modes of substrates with both enzymes were also compared. The calculated docking interaction energy of trihydroxybenzoic acid related compounds shows high\r\naffinity, suggesting specificity and potential use as common inhibitor to grape ascorbate\r\nperoxidase and polyphenol oxidase
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