Literature summary for 2.2.1.2 extracted from

Schorken, U.; Jia, J.; Sahm, H.; Sprenger, G.A.; Schneider, G.
Disruption of Escherichia coli transaldolase into catalytically active monomers: evidence against half-of-the-sites mechanism (1998), FEBS Lett., 441, 247-250.

Search for more literature for 2.2.1.2

Protein Variants

Protein Variants	Comment	Organism
R300A	little lower activity than the wild type, but same stability against urea and thermal inactivation	Escherichia coli
R300E	little lower activity than the wild type, but same stability against urea and thermal inactivation	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.265	-	D-erythrose 4-phosphate	R300A	Escherichia coli
0.295	-	D-erythrose 4-phosphate	wild-type	Escherichia coli
0.35	-	D-erythrose 4-phosphate	R300E	Escherichia coli
0.94	-	D-fructose 6-phosphate	wild-type	Escherichia coli
1.2	-	D-fructose 6-phosphate	R300E	Escherichia coli
1.35	-	D-fructose 6-phosphate	R300A	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)