CATH Classification

Domain Context

CATH Clusters

Superfamily alpha/beta hydrolase
Functional Family

Enzyme Information

2.3.1.94
6-deoxyerythronolide-B synthase.
based on mapping to UniProt Q03133
Propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH = 6-deoxyerythronolide B + 7 CoA + 6 CO(2) + H(2)O + 6 NADP(+).
-!- The product, 6-deoxyerythronolide B, contains a 14-membered lactone ring and is an intermediate in the biosynthesis of erythromycin antibiotics. -!- Biosynthesis of 6-deoxyerythronolide B requires 28 active sites that are precisely arranged along three large polypeptides, denoted DEBS1, -2 and -3. -!- The polyketide product is synthesized by the processive action of a loading didomain, six extension modules and a terminal thioesterase domain. -!- Each extension module contains a minimum of a ketosynthase (KS), an acyltransferase (AT) and an acyl-carrier protein (ACP). -!- The KS domain both accepts the growing polyketide chain from the previous module and catalyzes the subsequent decarboxylative condensation between this substrate and an ACP-bound methylmalonyl extender unit, introduce by the AT domain. -!- This combined effort gives rise to a new polyketide intermediate that has been extended by two carbon atoms.

UniProtKB Entries (1)

Q03133
ERYA3_SACER
Saccharopolyspora erythraea
6-deoxyerythronolide-B synthase EryA3, modules 5 and 6

PDB Structure

PDB 5D3K
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Towards a characterization of the structural determinants of specificity in the macrocyclizing thioesterase for deoxyerythronolide B biosynthesis.
Argyropoulos, P., Bergeret, F., Pardin, C., Reimer, J.M., Pinto, A., Boddy, C.N., Schmeing, T.M.
Biochim.Biophys.Acta