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Enzymatic Synthesis and Purification of Aromatic Coenzyme A Esters

✍ Scribed by Till Beuerle; Eran Pichersky

Publisher
Elsevier Science
Year
2002
Tongue
English
Weight
87 KB
Volume
302
Category
Article
ISSN
0003-2697

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✦ Synopsis

Two recombinant His-tagged proteins, a plant 4-coumarate:coenzyme A ligase (EC 6.2.1.12) and a bacterial benzoate:coenzyme A ligase (EC 6.2.1.25), were expressed in Escherichia coli and purified in a single step using Ni-chelating chromatography. Purified enzymes were used to synthesize cinnamoyl-coenzyme A (CoA), p-coumaroyl-CoA, feruloyl-CoA, caffeoyl-CoA, and benzoyl-CoA. Conversions up to 95% were achieved. Using a rapid solid-phase extraction procedure, the target CoA esters were isolated with yields of up to 80%. Structures were confirmed by analytical comparison with chemically synthesized reference compounds and electrospray ionization-mass spectrometry. The recombinant enzymes were stable for several months at ؊80°C, thus providing a reliable and facile method to produce these delicate biological intermediates.

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