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Literature summary extracted from

  • Baik, S.H.; Yoshioka, H.
    Enhanced synthesis of L-threo-3,4-dihydroxyphenylserine by high-density whole-cell biocatalyst of recombinant L-threonine aldolase from Streptomyces avelmitilis (2009), Biotechnol. Lett., 31, 443-448.
    View publication on PubMed

Application

EC Number Application Comment Organism
4.1.2.48 biotechnology a continuous bioconversion system for L-threo-3,4-dihydroxyphenylserine production is developed that uses whole-cell biocatalyst of recombinant Escherichia coli expressing L-TA genes cloned from Streptomyces avelmitilis MA-4680. Maximum conversion rates are observed at 2 M glycine, 145 mM 3,4-dihydroxybenzaldehyde, 0.75% Triton-X, 5 g Escherichia coli cells/l, pH 6.5 and 10°C. In the optimized condition, overall productivity is 8 g/l Streptomyces avermitilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.48 recombinantly expressed in Escherichia coli Streptomyces avermitilis

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.48 Streptomyces avermitilis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.48 glycine + 3,4-dihydroxybenzaldehyde
-
 Streptomyces avermitilis L-threo-3,4-dihydroxyphenylserine
-
 r

Synonyms

EC Number Synonyms Comment Organism
4.1.2.48 L-TA
-
 Streptomyces avermitilis
4.1.2.48 threonine aldolase
-
 Streptomyces avermitilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.2.48 10
-
-
 Streptomyces avermitilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.2.48 6.5
-
-
 Streptomyces avermitilis