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1. 小児における後天性末梢性ニューロパチーの概要 overview of acquired peripheral neuropathies in children
2. 水溶性ビタミンの概要 overview of water soluble vitamins
3. 持続的なアルコール依存症患者における栄養状態 nutritional status in patients with sustained heavy alcohol use
4. 小児の栄養障害と関連した微量栄養素欠乏 micronutrient deficiencies associated with malnutrition in children
5. メープルシロップ尿症の概要 overview of maple syrup urine disease

English Journal

Thiamine triphosphatase and the CYTH superfamily of proteins.

Bettendorff L1, Wins P.Author information 1GIGA-Neuroscience, University of Liège, Belgium.AbstractThe 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, archaeons, 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 superfamily 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 (β-barrel) conformation. The Nitrosomonas europaea, Escherichia coli and Arabidopsis thaliana CYTH proteins are specific inorganic tripolyphosphatases. We propose that inorganic tripolyphosphate, the simplest triphosphate compound, is the primitive substrate of CYTH proteins, other enzyme activities, such as adenylate cyclase (in A. hydrophila and Yersinia pestis), mRNA triphosphatase (in fungi and protozoans), and ThTPase (in metazoans), being secondary acquisitions. ThTPase activity is not limited to mammals, as sea anemone and zebrafish CYTH proteins are specific ThTPases. The acquisition of this enzyme activity is linked to the presence of a tryptophan involved in the binding of the thiazolium heterocycle of the thiamine molecule. Furthermore, we propose a conserved catalytic mechanism between a bacterial inorganic tripolyphosphatase and metazoan ThTPases, based on a catalytic dyad comprising a lysine and a tyrosine, explaining the alkaline pH optimum of these enzymes.
The FEBS journal.FEBS J.2013 Dec;280(24):6443-55. doi: 10.1111/febs.12498. Epub 2013 Sep 10.
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, archaeons, fungi, plants, and a
PMID 24021036

Structural determinants of specificity and catalytic mechanism in mammalian 25-kDa thiamine triphosphatase.

Delvaux D1, Kerff F, Murty MR, Lakaye B, Czerniecki J, Kohn G, Wins P, Herman R, Gabelica V, Heuze F, Tordoir X, Marée R, Matagne A, Charlier P, De Pauw E, Bettendorff L.Author information 1GIGA-Neurosciences, Université de Liège, Avenue de l'Hôpital 1, Liège, Belgium.AbstractBACKGROUND: Thiamine triphosphate (ThTP) is present in most organisms and might be involved in intracellular signaling. In mammalian cells, the cytosolic ThTP level is controlled by a specific thiamine triphosphatase (ThTPase), belonging to the CYTH superfamily of proteins. CYTH proteins are present in all superkingdoms of life and act on various triphosphorylated substrates.
Biochimica et biophysica acta.Biochim Biophys Acta.2013 Oct;1830(10):4513-23. doi: 10.1016/j.bbagen.2013.05.014. Epub 2013 May 22.
BACKGROUND: Thiamine triphosphate (ThTP) is present in most organisms and might be involved in intracellular signaling. In mammalian cells, the cytosolic ThTP level is controlled by a specific thiamine triphosphatase (ThTPase), belonging to the CYTH superfamily of proteins. CYTH proteins are present
PMID 23707715

[Existence of two different active sites on thiamine binding protein in plasma membranes of synaptosomes].

Parkhomenko IuM, Strokina AA, Pilipchuk SIu, Stepanenko SP, Chekhovskaia LI, Donchenko GV.AbstractThe current work is aimed at understanding the structure and functionality of thiamine binding protein (TBP) in neural cells plasma membranes. The influence of thiamine triphosphate on thiamine binding by TBP in synaptic plasma membranes (SPM) isolated from the rat brain was investigated. It was shown that thiamine triphosphate inhibits thiamine binding activity of SPM in concurrent manner (K(i) = 1.0 +/- 0.3 microM). At the same time thiamine had no effect on thiamine triphosphatase (ThTPase) activity at the concentration range 0.5-20 microM. Otherwise, ThTPase activation with the maximum at the concentration about 2.5 microM was observed. Further, the influence of classic thiamine antagonists (amprolium, oxythiamine and pyrithiamine) on both biological activities of TBP in SPM was studied. The IC50 value for inhibition of thiamine binding on SPM by amprolium comprised 50 +/- 4.0 microM. Still, this antagonist had no effect on ThTPase activity. For the oxythiamine inhibition of both TBP activities was detected. The values of IC50 were 125 +/- 28 and 1000 +/- 95 microM for thiamine binding and ThTPase activity, respectively. The values of IC50 for thiamine binding and ThTPase activity inhibition differed by more than one order of magnitude and comprised 2.2 +/- 0.2 and 43 +/- 9 microM, respectively. The obtained data indicate that the active sites on SPM responsible for thiamine binding and ThTPase activity have different sensitivity to thiamine antagonists. Our results allow us to suppose that different active protein sites are responsible for the specific binding and for thiamine phosphates hydrolysis by TBP of synaptic membranes.
Ukrainskiĭ biokhimicheskiĭ zhurnal.Ukr Biokhim Zh.2010 Jan-Feb;82(1):34-41.
The current work is aimed at understanding the structure and functionality of thiamine binding protein (TBP) in neural cells plasma membranes. The influence of thiamine triphosphate on thiamine binding by TBP in synaptic plasma membranes (SPM) isolated from the rat brain was investigated. It was sho
PMID 20684226

Japanese Journal

Thiamin Triphosphatase and Conducting Sites

SCHOFFENIELS E.
Journal of Nutritional Science and Vitaminology 38(Special), 387-391, 1992
NAID 130001369604

(Na^++K^+)-Adenosinetriphosphatase(ATPase)アイソザイムの生理的意義

松田敏夫
藥學雜誌 110(4), 235-245, 1990-04-25
… Since Sweadner demonstrated that there are two isozymes (α and α (+) isoforms) of (Na^++K^+)-adenosine triphosphatase (ATPase) in the brain about 10 years ago, the isozymes have been extensively studied at biochemical and molecular levels. … We started the studies on the isozymes of (Na^++K^+)-ATPase soon after finding that pyrithiamin, an antimetabolite of thiamin is a selective inhibitor of the α (+) isoform. …
NAID 110003650000

Hydrolysis and synthesis of thiamin triphosphate in bacteria.

西宗高弘,林良二
Journal of Nutritional Science and Vitaminology 33(2), 113-127, 1987
… Thiamin triphosphate (ThTP) in early stationary phase cells of Escherichia coli grown in nutrient broth with 0.1% yeast extract was found to constitute approximately 5-7% of cellular thiamin diphosphate (ThDP) or around 5 nmol/g cell. … Two phosphatases specific for ThTP (ThTPase) among thiamin phosphates were detected in E. …
NAID 130001370739