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Literature summary for 2.7.11.27 extracted from

  • Jamil, H.; Madsen, N.B.
    Phosphorylation state of acetyl-coenzyme A carboxylase. I. Linear inverse relationship to activity ratios at different citrate concentrations (1987), J. Biol. Chem., 262, 630-637.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [acetyl-CoA carboxylase] Rattus norvegicus phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis ADP + [acetyl-CoA carboxylase] phosphate
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Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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-
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Purification (Commentary)

Purification (Comment) Organism
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Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
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Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [acetyl-CoA carboxylase] inactivation of carboxylase Rattus norvegicus ADP + [acetyl-CoA carboxylase] phosphate
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?
ATP + [acetyl-CoA carboxylase] incorporates 0.45 mol phosphate per mol of carboxylase Rattus norvegicus ADP + [acetyl-CoA carboxylase] phosphate
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?
ATP + [acetyl-CoA carboxylase] phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis Rattus norvegicus ADP + [acetyl-CoA carboxylase] phosphate
-
?