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Literature summary for 4.1.2.48 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

Application Comment Organism
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)

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

Organism

Organism UniProt Comment Textmining
Streptomyces avermitilis
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
L-TA
-
Streptomyces avermitilis
threonine aldolase
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Streptomyces avermitilis

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
Streptomyces avermitilis