Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes

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 sm...

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Autor principal:	Lucien Bettendorff
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	thiamine triphosphate adenosine thiamine triphosphate thiamine triphosphatase adenylate kinase CYTH triphosphate tunnel metalloenzymes Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/3d80d9aaf84c4deda2eccf57c9406e26
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spelling	oai:doaj.org-article:3d80d9aaf84c4deda2eccf57c9406e262021-11-25T16:53:20ZUpdate on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes10.3390/biom111116452218-273Xhttps://doaj.org/article/3d80d9aaf84c4deda2eccf57c9406e262021-11-01T00:00:00Zhttps://www.mdpi.com/2218-273X/11/11/1645https://doaj.org/toc/2218-273XWhile 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 <i>E. coli</i>, ThTP is synthesized during amino acid starvation, while in plants, its synthesis is dependent on photosynthetic processes. In <i>E. coli</i>, 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 <i>thtpa</i>, 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 <i>E. coli</i>, 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.Lucien BettendorffMDPI AGarticlethiamine triphosphateadenosine thiamine triphosphatethiamine triphosphataseadenylate kinaseCYTHtriphosphate tunnel metalloenzymesMicrobiologyQR1-502ENBiomolecules, Vol 11, Iss 1645, p 1645 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	thiamine triphosphate adenosine thiamine triphosphate thiamine triphosphatase adenylate kinase CYTH triphosphate tunnel metalloenzymes Microbiology QR1-502
spellingShingle	thiamine triphosphate adenosine thiamine triphosphate thiamine triphosphatase adenylate kinase CYTH triphosphate tunnel metalloenzymes Microbiology QR1-502 Lucien Bettendorff Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes
description	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 <i>E. coli</i>, ThTP is synthesized during amino acid starvation, while in plants, its synthesis is dependent on photosynthetic processes. In <i>E. coli</i>, 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 <i>thtpa</i>, 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 <i>E. coli</i>, 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.
format	article
author	Lucien Bettendorff
author_facet	Lucien Bettendorff
author_sort	Lucien Bettendorff
title	Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes
title_short	Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes
title_full	Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes
title_fullStr	Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes
title_full_unstemmed	Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes
title_sort	update on thiamine triphosphorylated derivatives and metabolizing enzymatic complexes
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/3d80d9aaf84c4deda2eccf57c9406e26
work_keys_str_mv	AT lucienbettendorff updateonthiaminetriphosphorylatedderivativesandmetabolizingenzymaticcomplexes
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Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes

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