Protein Variants | Comment | Organism |
---|---|---|
additional information | site-directed mutagenesis to identify ACP residues that contribute to the observed specificity. Module 3 of the 6-deoxyerythronolide B synthase is reengineered to catalyze two successive rounds of chain elongation | Saccharopolyspora erythraea |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Saccharopolyspora erythraea | unidirectional translocation of the growing polyketide chain along the 6-deoxyerythronolide B synthase, ratchet mechanism, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharopolyspora erythraea | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | unidirectional translocation of the growing polyketide chain along the 6-deoxyerythronolide B synthase, ratchet mechanism, overview | Saccharopolyspora erythraea | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | solution structure of ACP2, the tertiary fold of ACP2 is a three-helix bundle, overview | Saccharopolyspora erythraea |
Synonyms | Comment | Organism |
---|---|---|
6-deoxyerythronolide B synthase | - |
Saccharopolyspora erythraea |
General Information | Comment | Organism |
---|---|---|
additional information | enzyme-substrate interactions are involved in the translocation of a polyketide from ACP2 to ketosynthase KS3, the ACP domain of the 6-deoxyerythronolide B synthase contributes to its association with its ketosynthase, KS, translocation partner, models for KS-ACP recognition during chain elongation and chain translocation, docking model, overview. Determination of selective proteinprotein interactions between the two partners using CF3-S-ACP as probe. The acyl chain substrate also has a significant influence on this interaction | Saccharopolyspora erythraea |