Function and Biology Details
Reactions catalysed:
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH
An acyl-[acyl-carrier protein] + NADP(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein]
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein]
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]
Acetyl-CoA + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + (n+1) CoA + n CO(2) + 2n NADP(+)
Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-carrier-protein] + oleate
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H(2)O
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Fatty acid synthase (preferred)
PDBe Complex ID:
PDB-CPX-146317 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fatty acid synthase
Molecule details ›
Chain: A
Length: 89 amino acids
Theoretical weight: 9.7 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Phosphopantetheine attachment site
Structure domains: ACP-like
Length: 89 amino acids
Theoretical weight: 9.7 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P12785 (Residues: 2114-2202; Coverage: 4%)
Sequence domains: Phosphopantetheine attachment site
Structure domains: ACP-like
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
80%
Refinement method:
simulated annealing
Expression system: Escherichia coli BL21(DE3)
