Literature summary for 6.3.4.14 extracted from

Cho, Y.S.; Lee, J.I.; Shin, D.; Kim, H.T.; Jung, H.Y.; Lee, T.G.; Kang, L.W.; Ahn, Y.J.; Cho, H.S.; Heo, Y.S.
Molecular mechanism for the regulation of human ACC2 through phosphorylation by AMPK (2010), Biochem. Biophys. Res. Commun., 391, 187-192.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of the biotin carboxylase domain of human acetyl-CoA carboxylase ACC2 phosphorylated by AMP-activated protein kinase AMPK. The phosphorylated Ser222 binds to the putative dimer interface of biotin carboxylase, disrupting polymerization and providing the molecular mechanism of inactivation by AMPK. The structure of the biotin carboxylase domain in complex with soraphen A, a macrocyclic polyketide natural product, shows that the compound binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMPK	Homo sapiens

Crystallization (Comment)

Organism

crystal structures of the biotin carboxylase domain of human acetyl-CoA carboxylase ACC2 phosphorylated by AMP-activated protein kinase AMPK. The phosphorylated Ser222 binds to the putative dimer interface of biotin carboxylase, disrupting polymerization and providing the molecular mechanism of inactivation by AMPK. The structure of the biotin carboxylase domain in complex with soraphen A, a macrocyclic polyketide natural product, shows that the compound binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMPK

Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
soraphen A	macrocyclic polyketide natural product, binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMP-activated protein kinase	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O00763	-	-

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Release 2023.1 (January 2023)