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- W2285345462 abstract "Introduction: The enzyme, Phenylalanine dehydrogenase (L-phe DH; NAD oxidoreductase, deaminating; EC 1.4.1.20) belongs to the amino acid dehydrogenase family of enzymes which catalyzes the reversible oxidative deamination reaction of L-phenylalanine to their respective α- ketoacids. An assay technique with a high sensitivity for blood L-phenylalanine level, an important marker for the screening of Phenylketonuria (PKU), has been established by means of PheDH. This enzyme is being used as a commercial and valuable biocatalyst in medical and pharmaceutical industries. The enzymes of this family are closely related in structure and function. Methods: Swiss-Pdb Viewer used for analysis and Rhodococcus sp. M4 was chosen because of the availability of several crystal structures with bound substrates and its high specific activity. Results : Rhodococcus sp. M4 and B. badius PheDHs are very different from each other on a sequence level, sharing only 32% identity and 50% similarity. Coming from the same structural sub-family, they share a much stronger correlation in their folding motifs. Conclusions: Since there currently is no crystal structure available for the B. badius PheDH, the sequence was folded over the 1BW9 crystal structure and superimposed over the original scaffold using SuperPose." @default.
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- W2285345462 date "2015-11-01" @default.
- W2285345462 modified "2023-09-27" @default.
- W2285345462 title "Evaluation of the active site of phenylalanine dehydrogenase isolated from Bacillus badius using homology based modeling" @default.
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- W2285345462 doi "https://doi.org/10.20286/focsci-01014" @default.
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