Literature summary for 5.3.1.1 extracted from

Solem, C.; Koebmann, B.; Jensen, P.R.
Control analysis of the role of triosephosphate isomerase in glucose metabolism in Lactococcus lactis (2008), IET Syst. Biol., 2, 64-72.

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Protein Variants

Protein Variants	Comment	Organism
additional information	modulation of gene expression around wild-type level by replacing the native promoter with libraries of synthetic promoters. Enzyme is present in high excess in wild-type cells. 10% residual activity still support more than 70% of the wild-type glycolytic flux. At at residual triosephosphate isomerase activity of 3%, dihydroxyacetone phosphate level increases four times and coincides with an increase in formate production	Lactococcus lactis

Organism

Organism	UniProt	Comment	Textmining
Lactococcus lactis	-	ssp. Lactis IL403. Enzyme is present in high excess in wild-type cells. 10% residual activity still support more than 70% of the wild-type glycolytic flux. At at residual triosephosphate isomerase activity of 3%, dihydroxyacetone phosphate level increases four times and coincides with an increase in formate production	-

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Release 2023.1 (January 2023)