CATH Classification

Domain Context

CATH Clusters

Superfamily 6.10.40.10
Functional Family

Enzyme Information

2.3.1.94
6-deoxyerythronolide-B synthase.
based on mapping to UniProt Q03132
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)

Q03132
ERYA2_SACER
Saccharopolyspora erythraea
6-deoxyerythronolide-B synthase EryA2, modules 3 and 4

PDB Structure

PDB 1PZR
External Links
Method SOLUTION NMR
Organism Escherichia
Primary Citation
The structure of docking domains in modular polyketide synthases.
Broadhurst, R.W., Nietlispach, D., Wheatcroft, M.P., Leadlay, P.F., Weissman, K.J.
Chem.Biol.