Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces venezuelae | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
PikAI | - |
Streptomyces venezuelae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | enzyme utilizes an oxidized quinone as co-factor | Streptomyces venezuelae |
General Information | Comment | Organism |
---|---|---|
physiological function | in modular type I polyketide synthases the presence of the three processing domains, i.e. ketoreductase (KR), dehydratase (DH), and enoylreductase (ER), are varied in each module, leading to a fully reduced, partially reduced, or unreduced segment on the polyketide chain. Dehydratase PikDH2 converts D-alcohol substrates to trans-olefin products. The reaction is reversible with equilibrium constants ranging from 1.2 to 2. The enzyme activity is robust, and PikDH2 can be used for the chemoenzymatic synthesis of unsaturated triketide products. PikDH2 shows remarkably strict substrate specificity and is unable to turn over substrates that are epimeric at the beta-, gamma-, or delta-position | Streptomyces venezuelae |