A novel enzyme, d-3-hydroxyaspartate aldolase from Paracoccus denitrificans IFO 13301: purification, characterization, and gene cloning
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- Liu, J.Q., Dairi, T., Itoh, N. et al. Appl Microbiol Biotechnol (2003) 62: 53. doi:10.1007/s00253-003-1238-2
A novel enzyme, d-3-hydroxyaspartate aldolase (d-HAA), catalyzing the conversion of d-3-hydroxyaspartate to glyoxylate plus glycine, was purified to homogeneity from Paracoccus denitrificans IFO 13301. d-HAA is strictly d-specific as to the α-position, whereas the enzyme does not distinguish between threo and erythro forms at the β-position. In addition to d-3-hydroxyaspartate, the enzyme also acts on d-threonine, d-3-3,4-dihydroxyphenylserine, d-3-3,4-methylenedioxyphenylserine, and d-3-phenylserine. The d-HAA gene was cloned and sequenced. The gene contains an open reading frame consisting of 1,161 nucleotides corresponding to 387 amino acid residues. The predicted amino acid sequence displayed 35% and 22% identity with that of the d-threonine aldolase of Arthrobacer sp. DK-38 and Alcaligenes xylosoxidan IFO 12669, respectively. This is the first paper reporting both a purified enzyme with d-3-hydroxyaspartate aldolase activity and also its gene cloning.