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d-Amino Acid Dehydrogenases of Pseudomonas fluorescens

From the ¹ From the Department of Medical Chemistry, Kyoto University Faculty of Medicine, Kyoto, Japan

Two distinct d-amino acid dehydrogenases, each showing absolute specificity for methylene blue or 2,6-dichloroindophenol, respectively, were isolated from Pseudomonas fluorescens (ATCC 11299B).

The methylene blue-specific d-amino acid dehydrogenase was detectable only in extracts from d-tryptophan-grown cells and was purified about 40-fold. The 2,6-dichloroindophenol-specific d-amino acid dehydrogenase is constitutive, being present in all cell extracts irrespective of culture conditions, and it was purified about 65-fold.

These enzymes appear to be flavoproteins in which the flavin adenine dinucleotide prosthetic group is tightly bound to the enzyme protein.

The optimal pH of two enzymes was 7 to 8 and the Michaelis-Menten constant was 3 to 5 x 10^-4 m for each d-amino acid.

Substrate specificity and thermal stability were observed to be somewhat different for the two enzymes. No inhibition of these enzymes was observed with metal chelating agents.

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