Acetyl-CoA carboxylase

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'''Acetyl-CoA carboxylase''' (ACC) catalyzes the irreversible carboxylation of acetyl-CoA to malonyl-CoA. Malonyl-CoA is a building block in in the biosynthesis of fatty acids. ACC is biotin- and ATP-dependent enzyme. In mammals, 2 forms of ACC exist. ACC1 and ACC2 differ in their tissue distribution and function.
'''Acetyl-CoA carboxylase''' (ACC) catalyzes the irreversible carboxylation of acetyl-CoA to malonyl-CoA. Malonyl-CoA is a building block in in the biosynthesis of fatty acids. ACC is biotin- and ATP-dependent enzyme. In mammals, 2 forms of ACC exist. ACC1 and ACC2 differ in their tissue distribution and function.
== Structural highlights ==
== Structural highlights ==
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ACC is a multi-subunit enzyme in prokaryotes and plants. Each subunit catalyzes different reaction. These are – '''biotin carboxylase''' (BC) which carboxylates the biotin prosthetic group see [[Biotin carboxylase]], '''biotin carboxyl carrier protein''' (BCCP) which is linked covalently to biotin and '''carboxyltransferase''' (CT) which transfers the carboxyl group from biotin to acetyl-CoA. In eukaryotes these functions are performed by a single polypeptide chain. The biotindyl domain (residues 891-964 in human) transfers an activated carboxyl group from the BC domain to the CT domain.
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ACC is a multi-subunit enzyme in prokaryotes and plants. Each subunit catalyzes different reaction. These are – '''biotin carboxylase''' (BC) which carboxylates the biotin prosthetic group see [[Biotin carboxylase]], '''biotin carboxyl carrier protein''' (BCCP) which is linked covalently to biotin and '''carboxyltransferase''' (CT) which transfers the carboxyl group from biotin to acetyl-CoA. In eukaryotes these functions are performed by a single polypeptide chain. The biotindyl domain (residues 891-964 in human) transfers an activated carboxyl group from the BC domain to the CT domain. <scene name='49/492046/Cv/2'>E.coli biotin carboxylase complex with biotin</scene> ([[1bdo]]) is shown.
== Disease ==
== Disease ==

Revision as of 08:49, 2 November 2015

PDB ID 1bdo

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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