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Literature summary for 2.6.1.18 extracted from

  • Cardenas-Fernandez, M.; Neto, W.; Lopez, C.; Alvaro, G.; Tufvesson, P.; Woodley, J.M.
    Immobilization of Escherichia coli containing omega-transaminase activity in LentiKats (2012), Biotechnol. Prog., 28, 693-698.
    View publication on PubMed
Search for more literature for 2.6.1.18

Application

Application Comment Organism
biotechnology recombinant Escherichia coli cells containing overexpressed omega-TA activity are immobilized by entrapment in LentiKats and the effect of permeabilization on free cells and their immobilized counterparts is analyzed. Cells are applied in the synthesis of the aromatic amines 3-amino-1-phenylbutane and 1-phenylethylamine. The best results are obtained with CTAB 0.1% for permeabilization which results in an increase in reaction rate by 40% compared to the whole cells. The synthesis of 1-phenylethylamine is carried out using isopropyl amine and L-alanine as amino donors. Using whole cell biocatalysis, the reaction with isopropyl amine is one order of magnitude faster than with L-alanine Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-phenylethylamine + pyruvate
-
 Escherichia coli acetophenone + L-alanine
-
 r
4-phenyl-2-butanone + isopropylamine
-
 Escherichia coli 3-amino-1-phenylbutane + acetone
-
 ir

Synonyms

Synonyms Comment Organism
omega-transaminase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Escherichia coli