Abstract
A novel enzyme system that desaturates the side chain of the catecholamine derivative, N-acetyldopamine (NADA), was isolated and characterized from the larval cuticle of Sarcophaga bullata. The NADA desaturase system which converts NADA to 1,2-dehydro-NADA, surprisingly, does not resemble dehydrogenases such as succinate dehydrogenase. It uniquely performs the desaturation reaction by oxidizing NADA to its corresponding quinone and subsequently converting the resultant quinone to 1,2-dehydro-NADA via NADA quinone methide. Accordingly, desaturase enzyme preparation contained both o-diphenoloxidase activity and NADA quinone:NADA quinone methide isomerase activity. In addition, inhibition studies as well as trapping experiments also confirmed the obligatory formation of NADA quinone as the transient intermediate of the NADA desaturation. It is the first report of a cell-free system causing the side chain desaturation of any catecholamine derivative.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
