Acetyl-CoA carboxylase
| Acetyl-CoA carboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.4.1.2 | ||||||||
| CAS number | 9023-93-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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| Search | |
|---|---|
| PMC | articles |
| PubMed | articles |
| NCBI | proteins |
| Acetyl-CoA carboxylase alpha | |
|---|---|
| Identifiers | |
| Symbol | ACACA |
| Alt. symbols | ACAC, ACC1, ACCA |
| Entrez | 31 |
| HUGO | 84 |
| OMIM | 601557 |
| RefSeq | NM_198839 |
| UniProt | Q13085 |
| Other data | |
| EC number | 6.4.1.2 |
| Locus | Chr. 17 q21 |
| Acetyl-CoA carboxylase beta | |
|---|---|
| Identifiers | |
| Symbol | ACACB |
| Alt. symbols | ACC2, ACCB |
| Entrez | 32 |
| HUGO | 85 |
| OMIM | 200350 |
| RefSeq | NM_001093 |
| UniProt | O00763 |
| Other data | |
| EC number | 6.4.1.2 |
| Locus | Chr. 12 q24.1 |
Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme that catalyzes the irreversible carboxylation of acetyl-CoA to produce malonyl-CoA through its two catalytic activities, biotin carboxylase (BC) and carboxyltransferase (CT). ACC is a multi-subunit enzyme in most prokaryotes and in the chloroplasts of most plants and algae, whereas it is a large, multi-domain enzyme in the endoplasmic reticulum of most eukaryotes. The most important function of ACC is to provide the malonyl-CoA substrate for the biosynthesis of fatty acids. The activity of ACC can be controlled at the transcriptional level as well as by small molecule modulators and covalent modification. The human genome contains the genes for two different ACCs — ACACA and ACACB.
Prokaryotes and plants have multi-subunit ACCs composed of several polypeptides encoded by distinct genes. Biotin carboxylase (BC) activity, biotin carboxyl carrier protein (BCCP), and carboxyl transferase (CT) activity are each contained on a different subunit. The stoichiometry of these subunits in the ACC holoenzyme differs amongst organisms.Humans and most eukaryotes have evolved an ACC with CT and BC catalytic domains and biotin carboxyl carrier domains on a single polypeptide. ACC functional regions, starting from the N-terminus to C-terminus are the biotin carboxylase (BC), biotin binding (BB), carboxyltransferase (CT), and ATP-binding (AB). AB lies within BC. Biotin is covalently attached through an amide bond to the long side chain of a lysine reside in BB. As BB is between BC and CT regions, biotin can easily translocate to both of the active sites where it is required.
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