Emissive Synthetic Cofactors: Enzymatic Interconversions of tzA Analogues of ATP, NAD+, NADH, NADP+, and NADPH. Issue 4 (21st December 2017)

• Record Type: Journal Article
• Authors: Hallé, François; Fin, Andrea; Rovira, Alexander R.; Tor, Yitzhak
• Is Part Of: Angewandte Chemie international edition. Volume 57:Issue 4(2018)
• Page Start: 1087
• Page End: 1090
• Publication Date: 2017-12-21
• Subjects: cofactors -- kinases -- NAD+ -- NADP+ -- nucleotides; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201711935
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: A series of enzymatic transformations, which generate visibly emissive isofunctional cofactors based on an isothiazolo[4, 3‐ d ]pyrimidine analogue of adenosine ( tz A ), was developed. Nicotinamide adenylyl transferase condenses nicotinamide mononucleotide and tz ATP to yieldN tz AD +, which can be enzymatically phosphorylated by NAD + kinase and ATP or tz ATP to the correspondingN tz ADP + . The latter can be engaged in NADP‐specific coupled enzymatic transformations involving conversion toN tz ADPH by glucose‐6‐phosphate dehydrogenase and reoxidation toN tz ADP + by glutathione reductase. TheN tz ADP + /N tz ADPH cycle can be monitored in real time by fluorescence spectroscopy. Abstract : Relatives in the spotlight : A series of enzymatic transformations generate visibly emissive isofunctional cofactors based on an isothiazolo[4, 3‐ d ]pyrimidine analogue of adenosine ( tz A, see figure). These synthetic cofactors may find utility as tools for monitoring redox reactions in vitro or potentially in living systems.