Literature summary for 4.1.2.13 extracted from

Koeck, T.; Levison, B.; Hazen, S.L.; Crabb, J.W.; Stuehr, D.J.; Aulak, K.S.
Tyrosine nitration impairs mammalian aldolase A activity (2004), Mol. Cell. Proteomics, 3, 548-557.

Search for more literature for 4.1.2.13

Inhibitors

Inhibitors	Comment	Organism	Structure
peroxynitrite	decrease of Vmax and KM for fructose-1,6-bisphosphate after incubation with peroxynitrite. Tyrosine residues in the carboxyl-terminal region of the aldolase are major targets of nitration. Tyrosine nitration of aldolase A can contribute to an impaired cellular glycolytic activity	Oryctolagus cuniculus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.1613	-	D-fructose 1,6-bisphosphate	-	Oryctolagus cuniculus

Organism

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	P00883	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
muscle	-	Oryctolagus cuniculus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-fructose 1,6-bisphosphate	-	Oryctolagus cuniculus	glycerone phosphate + D-glyceraldehyde 3-phosphate	-	?

Synonyms

Synonyms	Comment	Organism
aldolase A	-	Oryctolagus cuniculus

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)