Literature summary for 2.7.11.27 extracted from

Rubink, D.S.; Winder, W.W.
Effect of phosphorylation by AMP-activated protein kinase on palmitoyl-CoA inhibition of skeletal muscle acetyl-CoA carboxylase (2005), J. Appl. Physiol., 98, 1221-1227.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + [acetyl-CoA carboxylase]	Rattus norvegicus	acetyl-CoA carboxylase from skeletal muscle is more potently inhibited by palmitoyl-CoA after having been phosphorylated by AMPK. This may contribute to low muscle malonyl-CoA values and increasing fatty acid oxidation rates during long-term exercise when plasma fatty acid concentrations are elevated	ADP + [acetyl-CoA carboxylase] phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Rattus norvegicus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + [acetyl-CoA carboxylase]	-	Rattus norvegicus	ADP + [acetyl-CoA carboxylase] phosphate	-	?
ATP + [acetyl-CoA carboxylase]	acetyl-CoA carboxylase from skeletal muscle is more potently inhibited by palmitoyl-CoA after having been phosphorylated by AMPK. This may contribute to low muscle malonyl-CoA values and increasing fatty acid oxidation rates during long-term exercise when plasma fatty acid concentrations are elevated	Rattus norvegicus	ADP + [acetyl-CoA carboxylase] phosphate	-	?

Synonyms

Synonyms	Comment	Organism
AMPK	-	Rattus norvegicus

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Release 2023.1 (January 2023)