Enhanced synthesis of L-threo-3,4-dihydroxyphenylserine by high-density whole-cell biocatalyst of recombinant L-threonine aldolase from Streptomyces avelmitilis

Biotechnol Lett. 2009 Mar;31(3):443-8. doi: 10.1007/s10529-008-9885-0. Epub 2008 Nov 28.

Abstract

L-threo-3,4-Dihydroxyphenylserine (DOPS) is a chiral unnatural beta-hydroxy amino acid used for the treatment of Parkinson disease. We developed a continuous bioconversion system for DOPS production that uses whole-cell biocatalyst of recombinant Escherichia coli expressing L-threonine aldolase (L-TA) genes cloned from Streptomyces avelmitilis MA-4680. Maximum conversion rates were observed at 2 M glycine, 145 mM 3,4-dihydroxybenzaldehyde, 0.75% Triton-X, 5 g E. coli cells/l, pH 6.5 and 10 degrees C. In the optimized condition, overall productivity was 8 g/l, which represents 40 times the synthesis yield possible with no optimization of conditions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antiparkinson Agents / metabolism*
  • Benzaldehydes / metabolism
  • Biotechnology / methods*
  • Catechols / metabolism
  • Droxidopa / metabolism*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Glycine / metabolism
  • Glycine Hydroxymethyltransferase / genetics
  • Glycine Hydroxymethyltransferase / metabolism*
  • Streptomyces / enzymology*
  • Streptomyces / genetics
  • Threonine / metabolism*

Substances

  • Antiparkinson Agents
  • Benzaldehydes
  • Catechols
  • Threonine
  • protocatechualdehyde
  • Glycine Hydroxymethyltransferase
  • Droxidopa
  • Glycine