Evaluation of the Active Site of PhenylalanineDehydrogenase Isolated from Bacillus badius usingHomology Based Modeling

Introduction: The enzyme, Phenylalanine dehydrogenase (L-phe DH; NADoxidoreductase, deaminating; EC 1.4.1.20) belongs to the amino acid dehydrogenasefamily of enzymes which catalyzes the reversible oxidative deamination reaction ofL-phenylalanine to their respective α- ketoacids. An assay technique with a high sensitivityfor 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 acommercial and valuable biocatalyst in medical and pharmaceutical industries. Theenzymes of this family are closely related in structure and function.Methods: Swiss-Pdb Viewer used for analysis and Rhodococcus sp. M4 was chosen becauseof the availability of several crystal structures with bound substrates and its high specificactivity.Results: Rhodococcus sp. M4 and B. badius PheDHs are very different from each other ona sequence level, sharing only %32 identity and %50 similarity. Coming from the samestructural sub-family, they share a much stronger correlation in their folding motifs.Conclusions: Since there currently is no crystal structure available for the B. badiusPheDH, the sequence was folded over the 1BW9 crystal structure and superimposed overthe original scaffold using SuperPose.

کلیدواژه ها:

Phenylalanine Dehydrogenaseα-ketoacidsStructureFunctionSuperPose