Literature summary for 6.3.4.14 extracted from

Shen, Y.; Volrath, S.L.; Weatherly, S.C.; Elich, T.D.; Tong, L.
A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product (2004), Mol. Cell, 16, 881-891.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of biotin carboxylase domain of acetyl-coenzyme A carboxylase in Escherichia coli	Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the recombinant biotin carboxylase domain alone and in complex with soraphen A, sitting drop vapor diffusion method, crystals belong to space group P2(1), with cell parameters of a = 63.83 A, b = 96.52 A, c = 139.95 A and beta = 96.82 A	Saccharomyces cerevisiae

Inhibitors

Inhibitors	Comment	Organism	Structure
soraphen A	nanomolar inhibitor against biotin carboxylase domain of acetyl-coenzyme A carboxylase. The inhibitor may bind in the biotin carboxylase dimer interface and inhibits the biotin carboxylase activity by disrupting the oligomerization of the domain	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	Q00955	-	-

Synonyms

Synonyms	Comment	Organism
biotin carboxylase	domain of acetyl-coenzyme A carboxylase	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)