Applied Microbiology and Biotechnology

, Volume 49, Issue 6, pp 702–708

Low-specificity l-threonine aldolase of Pseudomonas sp. NCIMB 10558: purification, characterization and its application to β-hydroxy-α-amino acid synthesis

  • J. Q. Liu
  • S. Ito
  • T. Dairi
  • N. Itoh
  • S. Shimizu
  • H. Yamada
ORIGINAL PAPER

DOI: 10.1007/s002530051235

Cite this article as:
Liu, J., Ito, S., Dairi, T. et al. Appl Microbiol Biotechnol (1998) 49: 702. doi:10.1007/s002530051235

Abstract

Low-specificity l-threonine aldolase, catalyzing the reversible cleavage/condensation reaction between l-threonine/l-allo-threonine and glycine plus acetaldehyde, was purified to homogeneity from Pseudomonas sp. NCIMB 10558. The enzyme has an apparent molecular mass of approximately 145 kDa and consists of four identical subunits with a molecular mass of 38 kDa. The enzyme, requiring pyridoxal- 5′-phosphate as a coenzyme, is strictly l-specific at the α position, whereas it can not distinguish between threo and erythro forms at the β position. Besides the reversible cleavage/condensation of threonine, the enzyme also catalyzes the reversible interconversion between glycine plus various aldehydes and l-β-hydroxy-α-amino acids, including l-β-(3,4-dihydroxyphenyl)serine, l-β-(3,4-met‐hylenedioxyphenyl)serine and l-β-phenylserine, providing a new route for the industrial production of these important amino acids.

Copyright information

© Springer-Verlag Berlin Heidelberg 1998

Authors and Affiliations

  • J. Q. Liu
    • 1
  • S. Ito
    • 1
  • T. Dairi
    • 1
  • N. Itoh
    • 1
  • S. Shimizu
    • 2
  • H. Yamada
    • 1
  1. 1.Laboratory of Biocatalytic Chemistry, Biotechnology Research Center, Toyama Prefectural University, Kurokawa 5180, Kosugi Machi, Toyama 939-03, Japan Tel.: +81 766 56 7500 Fax: +81 766 56 2498 e-mail: ryu@pu-toyama.ac.jpJP
  2. 2.Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, JapanJP