Description
The enzyme from Thauera aromatica is a membrane-bound molybdenum-iron-sulfur protein. The enzyme is specific for phenylacetyl-CoA as substrate. Phenylacetate, acetyl-CoA, benzoyl-CoA, propanoyl-CoA, crotonyl-CoA, succinyl-CoA and 3-hydroxybenzoyl-CoA cannot act as substrates. The oxygen atom introduced into the product, phenylglyoxylyl-CoA, is derived from water and not molecular oxygen. Duroquinone, menaquinone and 2,6-dichlorophenolindophenol (DCPIP) can act as acceptor, but the likely physiological acceptor is ubiquinone. A second enzyme, EC 3.1.2.25, phenylacetyl-CoA hydrolase, converts the phenylglyoxylyl-CoA formed into phenylglyoxylate.
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