Establishment and characterization of a new class of adenylate cyclases (class VII ACs) in plants.

Adenylate cyclase is the key enzyme in the synthesis of cAMP. Now, more and more plant genes which possessing AC function are being identified, but the classification of plant ACs has not yet been systematically studied and the relationship of plant ACs with other existing six classes ACs in animals and microorganisms is still unclear. In this study, we found that 7 of the 15 reported plant ACs with conserved CYTH-like_AC_Ⅳ-like domain were clustered into a group with high confidence (Group Ⅳ), while the other plant ACs were clustered into other three groups with no common domain. In addition, we also found that the Group Ⅳ plant ACs were grouped into an independent and specific class (Class VII), separated from the existing six classes of ACs. The Group Ⅳ plant ACs, compared to the existing six classes of ACs, own unique CYTH-like_AC_Ⅳ-like conserved domain and EXEXK signature motif, characteristic protein tertiary structures, specific subcellular localization and catalytic conditions. In view of the above, we regarded the Group Ⅳ plant ACs as the seventh class of AC (VII AC). This study does the systematic classification of plant ACs which could lay a foundation for further identification and study of the biological functions of the plant-specific VII ACs.

Site-selective C-H alkylation of myo-inositol via organic photoredox catalysis.

Site-selective photoredox reactions with aromatic olefins enable direct alkylation of unprotected myo-inositol at C4. The efficacy of these reactions can be finely tuned by modifying the structures of HAT reagents. These reactions open the possibility of selective C-H alkylations of myo-inositol without the need for multi-step protection-deprotection strategies.