Applied Microbiology and Biotechnology

, Volume 62, Issue 1, pp 53–60

A novel enzyme, d-3-hydroxyaspartate aldolase from Paracoccus denitrificans IFO 13301: purification, characterization, and gene cloning

  • J. Q. Liu
  • T. Dairi
  • N. Itoh
  • M. Kataoka
  • S. Shimizu
Original Paper

DOI: 10.1007/s00253-003-1238-2

Cite this article as:
Liu, J.Q., Dairi, T., Itoh, N. et al. Appl Microbiol Biotechnol (2003) 62: 53. doi:10.1007/s00253-003-1238-2

Abstract

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.

Copyright information

© Springer-Verlag 2003

Authors and Affiliations

  • J. Q. Liu
    • 1
    • 3
  • T. Dairi
    • 1
  • N. Itoh
    • 1
  • M. Kataoka
    • 2
  • S. Shimizu
    • 2
  1. 1.Biotechnology Research CenterToyama Prefectural UniversityKosugiJapan
  2. 2.Division of Applied Life Sciences, Graduate School of AgricultureKyoto UniversityKyotoJapan
  3. 3.Analytical and Microbiology Department, Kobe Technical CenterProcter and Gamble Far EastKobeJapan