Abstract
The fatty acid photodecarboxylase from Chlorella variabilis NC64 A (CvFAP) catalyses the light‐dependent decarboxylation of fatty acids. Photoinactivation of CvFAP still represents one of the major limitations of this interesting enzyme en route to practical application. In this study we demonstrate that the photostability of CvFAP can easily be improved by the administration of medium‐chain length carboxylic acids such as caprylic acid indicating that the best way of maintaining CvFAP stability is ‘to keep the enzyme busy’.
Highlights
In this study we demonstrate that the photostability of CvFAP can be improved by the administration of medium-chain length carboxylic acids such as caprylic acid indicating that the best way of maintaining CvFAP stability is ‘to keep the enzyme busy’
The photoexcited flavin adenine dinucleotide (FAD) cofactor (1FAD*) inside the enzyme abstracts a single electron from the active site-bound carboxylate substrate resulting in the FAD semiquinone radical (FAD*À ) and carboxyl radical
Catalytic cycle of the photoenzymatic decarboxylation of carboxylic acids catalysed by the photodecarboxylase from Chlorella variabilis NC64A (CvFAP)
Summary
Stabilisation of the Fatty Acid Decarboxylase from Chlorella variabilis by Caprylic Acid. The fatty acid photodecarboxylase from Chlorella variabilis NC64 A (CvFAP) catalyses the light-dependent decarboxylation of fatty acids. The photoexcited FAD cofactor (1FAD*) inside the enzyme abstracts a single electron from the active site-bound carboxylate substrate resulting in the FAD semiquinone radical (FAD*À ) and carboxyl radical. Catalytic cycle of the photoenzymatic decarboxylation of carboxylic acids catalysed by the photodecarboxylase from Chlorella variabilis NC64A (CvFAP). From a CvFAP malfunction upon photoactivation in the absence of a carboxylate substrate In this situation, the photoexcited, high redox-potential flavin is assumed to oxidise nearby active site amino acid residues leading to irreversible inactivation of the enzyme. We set out to investigate whether the lightdependent inactivation of CvFAP may be alleviated by incubating the enzyme with carboxylic acids.
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