Reference : Thiamine triphosphatase and the CYTH family of proteins
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/151354
Thiamine triphosphatase and the CYTH family of proteins
English
Bettendorff, Lucien mailto [Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Biochimie et physiologie humaine et pathologique >]
Wins, Pierre [> >]
2013
FEBS Journal
Blackwell Publishing
280
24
6443–6455
Yes (verified by ORBi)
International
1742-464X
1742-4658
Oxford
United Kingdom
[en] thiamine ; triphosphatase ; tripolyphosphatase ; mRNA triphosphatase ; TTM
[en] The CYTH superfamily of proteins was named after its two founding members, the CYaB adenylyl cyclase from Aeromonas hydrophila and the human 25 kDa THiamine triphosphatase (ThTPase). Members of this superfamily of proteins exist in all organisms including bacteria, archaea, fungi, plants and animals (except birds) and can be traced back to the Last Universal Common Ancestor. Their sequences include several charged residues involved in divalent cation and triphosphate binding. Indeed, all members of the CYTH family that have been characterized act on triphosphorylated substrates and require at least one divalent metal cation for catalysis. In most cases, the enzyme-substrate complex adopts a tunnel-like (ß-barrel) conformation. The Nitrosomonas europaea and E.coli CYTH proteins are specific inorganic triphosphatases. We propose that inorganic triphosphate, the simplest triphosphate compound, is the primitive substrate of CYTH proteins. Other enzyme activities such as adenylate cyclase (in A. hydrophila and Y. pestis), mRNA triphosphatase (in fungi and protozoans) and ThTPase (in metazoans) are secondary acquisitions. ThTPase activity is not limited to mammals, but sea anemone and zebrafish CYTH proteins are already specific ThTPases and the acquisition of this enzyme activity is linked to the presence of a Trp (W53 in mammalian ThTPases) residue involved in the binding of the thiazole heterocycle of the thiamine molecule. Furthermore, we propose a conserved catalytic mechanism between a bacterial inorganic triphosphatase and metazoan ThTPases, based on a catalytic dyad comprising a Lys and a Tyr residue, explaining the alkaline pH optimum of these enzymes.
Giga-Neurosciences
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS
Researchers ; Students
http://hdl.handle.net/2268/151354
Contribution to the minireview series :
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<br />"Thiamine-dependent enzymes: new perspectives from the long-standing development on the interface of chemistry and biology''
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<br />Coordinated by V. Bunik

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