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Literature summary for 2.1.2.1 extracted from

  • Makart Stefa, M.S.; Heinemann Matthia, H.M.; Panke Sve, P.S.
    Characterization of the AlkS/P(alkB)-expression system as an efficient tool for the production of recombinant proteins in Escherichia coli fed-batch fermentations (2007), Biotechnol. Bioeng., 96, 326-336.
    View publication on PubMed

Application

Application Comment Organism
biotechnology the AlkS/PalkB-expression system is shown as an efficient tool for the production of recombinant serine hydroxymethyltransferase in Escherichia coli fed-batch fermentations Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
using the AlkS/PalkB-expression system Escherichia coli’s serine hydroxymethyltransferase gene glyA is overexpressed in Escherichia coli. It is shown that the system is already fully turned on at inducer concentrations as low as 0.005% (v/v). The optimum induction procedure for production of serine hydroxymethyltransferase is elaborated. Volumetric and specific productivity are found to increase with specific growth rate in glucose-limited fed-batch cultures. Acetate excretion as a result of recombinant protein production can be avoided in an optimized fermentation protocol by switching earlier to a linear feed. A final cell dry weight (CDW) concentration of 52 g/l is reached producing recombinant GlyA with a maximum specific activity of 6.3 U/mg total protein Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
maximal activity of 6.3 U/mg total protein is reached Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 3-phenylserine is used as a substrate Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
GlyA
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Escherichia coli
serine hydroxymethyltransferase
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Escherichia coli