CATH Classification
Level | CATH Code | Description |
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3 | Alpha Beta |
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3.30 | 2-Layer Sandwich |
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3.30.1490 | Dna Ligase; domain 1 |
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3.30.1490.20 | ATP-grasp fold, A domain |
Domain Context
CATH Clusters
Superfamily | ATP-grasp fold, A domain |
Functional Family | acetyl-CoA carboxylase isoform X1 |
Enzyme Information
6.4.1.2 |
Acetyl-CoA carboxylase.
based on mapping to UniProt O00763
ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA.
-!- This enzyme is a multi-domain polypeptide that catalyzes three different activities - a biotin carboxyl-carrier protein (BCCP), a biotin carboxylase that catalyzes the transfer of a carboxyl group from hydrogencarbonate to the biotin molecule carried by the carrier protein, and the transfer of the carboxyl group from biotin to acetyl-CoA, forming malonyl-CoA. -!- In some organisms these activities are catalyzed by separate enzymes (see EC 6.3.4.14 and EC 2.1.3.15). -!- The carboxylation of the carrier protein requires ATP, while the transfer of the carboxyl group to acetyl-CoA does not.
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6.3.4.14 |
Biotin carboxylase.
based on mapping to UniProt O00763
ATP + [biotin carboxyl-carrier protein]-biotin-N(6)-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]- carboxybiotin-N(6)-L-lysine.
-!- This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC 6.3.4.15. -!- In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. mycobacteria). -!- Yet in other organisms (e.g. mammals) this activity is included in a single polypeptide that also catalyzes the transfer of the carboxyl group from biotin to acetyl-CoA (see EC 6.4.1.2).
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UniProtKB Entries (1)
O00763 |
ACACB_HUMAN
Homo sapiens
Acetyl-CoA carboxylase 2
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PDB Structure
PDB | 5KKN |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Acetyl-CoA carboxylase inhibition by ND-630 reduces hepatic steatosis, improves insulin sensitivity, and modulates dyslipidemia in rats.
Proc.Natl.Acad.Sci.USA
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