Literature summary for 4.1.1.49 extracted from

Zamboni, N.; Maaheimo, H.; Szyperski, T.; Hohmann, H.P.; Sauer, U.
The phosphoenolpyruvate carboxykinase also catalyzes C3 carboxylation at the interface of glycolysis and the TCA cycle of Bacillus subtilis (2004), Metab. Eng., 6, 277-284.

Search for more literature for 4.1.1.49

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ADP + phosphoenolpyruvate + CO2	Bacillus subtilis	in contrast to its normal role in gluconeogenesis, PEP carboxykinase can operate in the reverse direction from phosphoenolpyruvate to oxaloacetate, upon knockout of pyruvate kinase in a riboflavin-producing Bacillus subtilis strain and in wild-type 168	ATP + oxaloacetate	-	r

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	riboflavin-producing strain and wild-type strain 168	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ADP + phosphoenolpyruvate + CO2	in contrast to its normal role in gluconeogenesis, PEP carboxykinase can operate in the reverse direction from phosphoenolpyruvate to oxaloacetate, upon knockout of pyruvate kinase in a riboflavin-producing Bacillus subtilis strain and in wild-type 168	Bacillus subtilis	ATP + oxaloacetate	-	r

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)