Reference : Thiamin diphosphate in biological chemistry: new aspects of thiamin metabolism, espe...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/11878
Thiamin diphosphate in biological chemistry: new aspects of thiamin metabolism, especially triphosphate derivatives acting other than as cofactors
English
Bettendorff, Lucien mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Biochimie et physiologie humaine et pathologique >]
Wins, Pierre [Université de Liège - ULG > GIGA-Neurosciences > > >]
2009
FEBS Journal
Blackwell Publishing
276
11
2917-2925
Yes (verified by ORBi)
International
1742-464X
Oxford
United Kingdom
[en] adenosine thiamine triphosphate ; adenylate kinase ; alarmone ; Escherichia coli ; thiamine triphoshate ; thiamine triphosphatase
[en] Prokaryotes, yeasts and plants synthesize thiamine (vitamin B1) via complex pathways. Animal cells capture the vitamin through specific high-affinity transporters essential for internal thiamine homeostasis. Inside the cells, thiamine is phosphorylated to higher phosphate derivatives. Thiamine diphosphate (ThDP) is the best-known thiamine compound for its role as an enzymatic cofactor. However, besides ThDP, at least three other thiamine phosphates occur naturally in most cells: thiamine monophosphate (ThMP), thiamine triphosphate (ThTP) and the recently discovered adenosine thiamine triphosphate (AThTP). It was suggested that ThTP has a specific neurophysiological role, but recent data are in favor of a much more basic metabolic function. During amino acid starvation, Escherichia coli accumulate ThTP possibly acting as a signal involved in the adaptation of the bacteria to changing nutritional conditions. In animal cells, ThTP can phosphorylate some proteins, but the physiological significance of this mechanism remains unknown. AThTP, recently discovered in E. coli, accumulates during carbon starvation and might act as an alarmone. Among the proteins involved in thiamine metabolism, thiamine transporters, thiamine pyrophosphokinase and a soluble 25-kDa thiamine triphosphatase have been characterized at the molecular level, in contrast to thiamine mono- and diphosphatases whose specificities remain to be proven. A soluble enzyme catalyzing the synthesis of AThTP from ThDP and ADP or ATP has been partially characterized in E. coli, but the mechanism of ThTP synthesis remains elusive. The data reviewed here illustrate the complexity of thiamine biochemistry, which is not restricted to the cofactor role of ThDP.
Giga-Neurosciences
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/11878
10.1111/j.1742-4658.2009.07019.x

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