Literature summary for 2.2.1.2 extracted from

Schorken, U.; Thorell, S.; Schurmann, M.; Jia, J.; Sprenger, G.A.; Schneider, G.
Identification of catalytically important residues in the active site of Escherichia coli transaldolase (2001), Eur. J. Biochem., 268, 2408-2415.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
D17A	lower specific activity than wild-type	Escherichia coli
E96A	lower specific activity than wild-type	Escherichia coli
N35A	lower specific activity than wild-type	Escherichia coli
S176A	lower specific activity than wild-type	Escherichia coli
T156A	lower specific activity than wild-type	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.078	-	D-erythrose 4-phosphate	T156A	Escherichia coli
0.1	-	D-erythrose 4-phosphate	wild-type, N35A	Escherichia coli
0.11	-	D-erythrose 4-phosphate	D17N	Escherichia coli
0.111	-	D-erythrose 4-phosphate	S176A	Escherichia coli
0.117	-	D-erythrose 4-phosphate	E96Q	Escherichia coli
0.122	-	D-erythrose 4-phosphate	E96A	Escherichia coli
0.555	-	D-erythrose 4-phosphate	D17A	Escherichia coli
0.6	-	D-fructose 6-phosphate	E96A	Escherichia coli
0.7	-	D-fructose 6-phosphate	D17A	Escherichia coli
0.96	-	D-fructose 6-phosphate	D17N	Escherichia coli
1.02	-	D-fructose 6-phosphate	T156A	Escherichia coli
1.1	-	D-fructose 6-phosphate	N35A	Escherichia coli
1.14	-	D-fructose 6-phosphate	E96Q	Escherichia coli
1.2	-	D-fructose 6-phosphate	wild-type	Escherichia coli
4.9	-	D-fructose 6-phosphate	S176A	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	K12	-

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Release 2023.1 (January 2023)