Journal
PHOTOCHEMISTRY AND PHOTOBIOLOGY
Volume 95, Issue 6, Pages 1376-1386Publisher
WILEY
DOI: 10.1111/php.13137
Keywords
-
Categories
Ask authors/readers for more resources
In the luminous ostracod Cypridina (presently Vargula) hilgendorfii, Cypridina luciferyl sulfate (3-enol sulfate of Cypridina luciferin) is converted to Cypridina luciferin by a sulfotransferase with 3 '-phosphoadenosine-5 '-phosphate (PAP) as a sulfate acceptor. The resultant Cypridina luciferin is used for the luciferase-luciferin reaction of Cypridina to emit blue light. The luminescence stimulation with major organic cofactors was examined using the crude extracts of Cypridina specimens, and we found that the addition of coenzyme A (CoA) to the crude extracts significantly stimulated luminescence intensity. Further, the light-emitting source in the crude extracts stimulated with CoA was identified as Cypridina luciferyl sulfate, and we demonstrated that CoA could act as a sulfate acceptor from Cypridina luciferyl sulfate. In addition, the sulfate group of Cypridina luciferyl sulfate was also transferred to adenosine 5 '-monophosphate (5 '-AMP) and adenosine 3 '-monophosphate (3 '-AMP) by a sulfotransferase. The sulfated products corresponding to CoA, 5 '-AMP and 3 '-AMP were identified using mass spectrometry. This is the first report that CoA can act as a sulfate acceptor in a sulfotransferase reaction.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available