Properties of chicken liver membrane-associated thiamine triphosphatase

Ik, Kolas; Af, Makarchikov

doi:10.15407/ubj87.03.037

Cited by 2 publications

(2 citation statements)

References 32 publications

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“…Thus, AThTP hydrolase has a quite high apparent affinity for substrate, like that of the specific soluble mammalian ThTPase (k m = 20-50 µМ [23]). For comparison, the k m values of non-specific phosphatases which might be involved in thiamine metabolism were reported to be 0.9 mM for ThMPase from chicken liver [24], 17-20.7 mM for ThDPase (NDPase) from rat and bovine liver [19,20], 2 mM for ThDPase (NDPase) from rat brain [20], 1.5-2.2 mM for a membrane-associated ThTPase in various animal species [25][26][27].…”

Section: Resultsmentioning

confidence: 99%

Adenosine thiamine triphosphate and adenosine thiamine triphosphate hydrolase activity in animal tissues

Makarchikov¹,

Saroka²,

Kudyrka³

2018

Ukr.Biochem.J.

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Adenosine thiamine triphosphate (AThTP), a vitamin B 1 containing nucleotide with unknown biochemical role, was found previously to be present in various biological objects including bacteria, yeast, some human, rat and mouse tissues, as well as plant roots. In this study we quantify AThTP in mouse, rat, bovine and chicken tissues. We also show that in animal tissues the hydrolysis of AThTP is catalyzed by a membranebound enzyme seemingly of microsomal origin as established for rat liver, which exhibits an alkaline ph optimum of 8.0-8.5 and requires no Mg 2+ ions for activity. In liver homogenates, AThTP hydrolase obeys Michaelis-Menten kinetics with apparent k m values of 84.4 ± 9.4 and 54.6 ± 13.1 µМ as estimated from the hanes plots for rat and chicken enzymes, respectively. The hydrolysis of AThTP has been found to occur in all samples examined from rat, chicken and bovine tissues, with liver and kidney being the most abundant in enzyme activity. In rat liver, the activity of AThTP hydrolase depends on the age of animals. k e y w o r d s: vitamin B 1 , adenosine thiamine triphosphate, adenosine thiamine triphosphate hydrolase, animal tissues.

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Section: Resultsmentioning

confidence: 99%

Adenosine thiamine triphosphate and adenosine thiamine triphosphate hydrolase activity in animal tissues

Makarchikov¹,

Saroka²,

Kudyrka³

2018

Ukr.Biochem.J.

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“…Very recently, the solubilization and the partial purification of the chicken liver enzyme was reported [ 67 ]. The ThTPase activity was coeluted with ATP and ITP hydrolyzing activities in a high molecular mass fraction and the K m for ThTP was about 2 mM.…”

Section: Thiamine Triphosphatasesmentioning

confidence: 99%

Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes

Bettendorff

2021

Biomolecules

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While the cellular functions of the coenzyme thiamine (vitamin B1) diphosphate (ThDP) are well characterized, the triphosphorylated thiamine derivatives, thiamine triphosphate (ThTP) and adenosine thiamine triphosphate (AThTP), still represent an intriguing mystery. They are present, generally in small amounts, in nearly all organisms, bacteria, fungi, plants, and animals. The synthesis of ThTP seems to require ATP synthase by a mechanism similar to ATP synthesis. In E. coli, ThTP is synthesized during amino acid starvation, while in plants, its synthesis is dependent on photosynthetic processes. In E. coli, ThTP synthesis probably requires oxidation of pyruvate and may play a role at the interface between energy and amino acid metabolism. In animal cells, no mechanism of regulation is known. Cytosolic ThTP levels are controlled by a highly specific cytosolic thiamine triphosphatase (ThTPase), coded by thtpa, and belonging to the ubiquitous family of the triphosphate tunnel metalloenzymes (TTMs). While members of this protein family are found in nearly all living organisms, where they bind organic and inorganic triphosphates, ThTPase activity seems to be restricted to animals. In mammals, THTPA is ubiquitously expressed with probable post-transcriptional regulation. Much less is known about the recently discovered AThTP. In E. coli, AThTP is synthesized by a high molecular weight protein complex from ThDP and ATP or ADP in response to energy stress. A better understanding of these two thiamine derivatives will require the use of transgenic models.

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Properties of chicken liver membrane-associated thiamine triphosphatase

Abstract: Энзимы, участвующие в метаболизме тиаминтрифосфата (ТТр)

Cited by 2 publications

References 32 publications

Adenosine thiamine triphosphate and adenosine thiamine triphosphate hydrolase activity in animal tissues

Adenosine thiamine triphosphate and adenosine thiamine triphosphate hydrolase activity in animal tissues

Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes

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