Table 1.
Composition of acyl-CoA carboxylase complexes in actinomycetes.
| Complex/ Organism |
ACCase (ACC) |
ACCase (PCC) |
ACCase (long substrate) |
ACCase? | ACCase? | ACCase? |
|---|---|---|---|---|---|---|
| Streptomyces | ||||||
| α: accA2 (accA1) | α: accA2 (accA1) | α: pccA | α: SCO4381 | |||
| β: accB | β: pccB | - | β: SCO2776 | β: SCO4380 | - | |
| ε: accE | ε: pccE | |||||
| Mycobacterium | ||||||
| α: accA3 | α: accA3 | α: accA3 | α: accA1 | α: accA2 | ||
| β: accD6 | β: accD5 | β: accD4 | β: accD1 | β: accD2 | β: accD3 | |
| ε: accE5 | β: accD5 | |||||
| Corynebacterium | ||||||
| α: accBC | α: accBC | α: accBC | ||||
| β: accD1 | β: accD2 | β: accD3 | ||||
| ε: accE | β: accD2 | - | - | β: accD4 | ||
| ε: accE |
ACCase: acyl-CoA carboxylase, ACC: acetyl-CoA carboxylase, PCC: propionyl-CoA carboxylase, α: subunit containing BC and BCCP domains, β: subunit containing CT domain, ε: small subunit necessary for maximal ACCase activity.