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.
Full Text 
Sign-in/Register to access full text options
Sign-in/Register to access full text options 
Paper version not known
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 call
