Literature summary for 2.3.1.240 extracted from

Li, Y.; Dodge, G.J.; Fiers, W.D.; Fecik, R.A.; Smith, J.L.; Aldrich, C.C.
Functional characterization of a dehydratase domain from the pikromycin polyketide synthase (2015), J. Am. Chem. Soc., 137, 7003-7006.

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Organism

Organism	UniProt	Comment	Textmining
Streptomyces venezuelae	-	-	-

Synonyms

Synonyms	Comment	Organism
PikAI	-	Streptomyces venezuelae

Cofactor

Cofactor	Comment	Organism	Structure
additional information	enzyme utilizes an oxidized quinone as cofactor	Streptomyces venezuelae

General Information

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

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Release 2023.1 (January 2023)