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Literature summary 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.
    View publication on PubMed

Inhibitors

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

Organism

EC Number Organism UniProt Comment Textmining
6.4.1.2 Escherichia coli
-
-
-
6.4.1.2 Staphylococcus aureus
-
-
-

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
6.4.1.2 ATP
-
 Staphylococcus aureus
6.4.1.2 ATP
-
 Escherichia coli