Literature summary extracted from

Herbert, D.; Price, L.J.; Alban, C.; Dehaye, L.; Job, D.; Cole, D.J.; Pallett, K.E.; Harwood, J.L.
Kinetic studies on two isoforms of acetyl-CoA carboxylase from maize leaves (1996), Biochem. J., 318, 997-1006.

Activating Compound

EC Number	Activating Compound	Comment	Organism	Structure
6.4.1.2	citrate	up to 1 mM no effect on isoform ACCase I activity, inhibitory above. 0.25-10 mM stimulates isoform ACCase 2 activity	Zea mays

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
6.4.1.2	Fluazifop	ACCase2 isoform is about 1/150 as sensitive as ACCase1 isoform	Zea mays
6.4.1.2	palmitoyl-CoA	-	Zea mays
6.4.1.2	Quizalofop	ACCase2 isoform is about 1/2000 as sensitive as ACCase1 isoform. Mixed-type inhibition of ACCase1 isoform with respect to acetyl-CoA or ATP	Zea mays

Organism

EC Number	Organism	UniProt	Comment	Textmining
6.4.1.2	Zea mays	-	major isoform ACCase 1 and a minor isoform ACCase 2	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
6.4.1.2	ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA	ordered mechanism	Zea mays	a

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
6.4.1.2	leaf	-	Zea mays	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
6.4.1.2	ATP + acetyl-CoA + HCO3-	-	Zea mays	ADP + phosphate + malonyl-CoA	-	?

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Release 2023.1 (January 2023)