Abstract
The pathway for vitamin B2 (riboflavin) biosynthesis in archaea contains several novel enzymes and reactions. The archaeal riboflavin kinase, RibK, is one such example – it has a unique structural fold, and phosphorylates B2 using CTP. Here, we characterize a new mesophilic archaeal RibK, compare its structure and function with a closely linked thermophilic homologue, and determine the molecular factors that confer thermal stability to this enzyme's characteristic structural fold. More information can be found in the Full Paper by Y. Kumar, R. K. Singh, and A. B. Hazra.
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