Literature summary for 6.4.1.2 extracted from

Bilder, P.; Lightle, S.; Bainbridge, G.; Ohren, J.; Finzel, B.; Sun, F.; Holley, S.; Al-Kassim, L.; Spessard, C.; Melnick, M.; Newcomer, M.; Waldrop, G.L.
The structure of the carboxyltransferase component of acetyl-CoA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme (2006), Biochemistry, 45, 1712-1722.

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Inhibitors

Inhibitors	Comment	Organism	Structure
moiramide B	potent inhibitor	Escherichia coli
moiramide B	potent inhibitor	Staphylococcus aureus

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Staphylococcus aureus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + acetyl-CoA + HCO3-	-	Staphylococcus aureus	ADP + phosphate + malonyl-CoA	-	?
ATP + acetyl-CoA + HCO3-	-	Escherichia coli	ADP + phosphate + malonyl-CoA	-	?

Synonyms

Synonyms	Comment	Organism
ACC	structural organization of the ACC multienzyme into distinct biotinoyl carboxyl carrier protein, biotin carboxylase, and carboxyltransferase components	Staphylococcus aureus
ACC	structural organization of the ACC multienzyme into distinct biotinoyl carboxyl carrier protein, biotin carboxylase, and carboxyltransferase components	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Staphylococcus aureus
ATP	-	Escherichia coli

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Release 2023.1 (January 2023)