関: thiamine pyrophosphate

WordNet

a coenzyme important in respiration in the Krebs cycle (同)thiamine_pyrophosphate

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/03/29 06:27:18」(JST)

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Thiamine pyrophosphate (TPP or ThPP), or thiamine diphosphate (ThDP), is a thiamine (vitamin B₁) derivative which is produced by the enzyme thiamine pyrophosphatase. Thiamine pyrophosphate is a cofactor that is present in all living systems, in which it catalyzes several biochemical reactions. It was first discovered as an essential nutrient (vitamin) in humans through its link with the peripheral nervous system disease Beriberi, which results from a deficiency of thiamine in the diet.^[1]

TPP works as a coenzyme in many enzymatic reactions, such as:

Pyruvate dehydrogenase complex^[2]
Pyruvate decarboxylase in ethanol fermentation
Alpha-ketoglutarate dehydrogenase complex
Branched-chain amino acid dehydrogenase complex
2-hydroxyphytanoyl-CoA lyase
Transketolase

Chemistry[edit]

The "ylid form" of TPP.

Chemically, TPP consists of a pyrimidine ring which is connected to a thiazole ring, which is in turn connected to a pyrophosphate (diphosphate) functional group.

The part of TPP molecule that is most commonly involved in reactions is the thiazole ring, which contains nitrogen and sulfur. Thus, the thiazole ring is the "reagent portion" of the molecule. The C2 of this ring is capable of acting as an acid by donating its proton and forming a carbanion. Normally, reactions that form carbanions are highly unfavorable, but the positive charge on the tetravalent nitrogen just adjacent to the carbanion stabilizes the negative charge, making the reaction more favorable. (A compound with positive and negative charges on adjacent atoms is called an ylid or ylide, so sometimes the carbanion form of TPP is referred to as the "ylid form".^[1]^[3]

Reaction mechanisms[edit]

In several reactions, including that of pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase, and transketolase, TPP catalyses the reversible cleavage of a substrate compound at a carbon-carbon bond connecting a carbonyl group to an adjacent reactive group (usually a carboxylic acid or an alcohol). It achieves this in four basic steps:

The carbanion of the TPP ylid nucleophilically attacks the carbonyl group on the substrate. (This forms a single bond between the TPP and the substrate.)
The target bond on the substrate is broken, and its electrons are pushed towards the TPP. This creates a double bond between the substrate carbon and the TPP carbon and pushes the electrons in the N-C double bond in TPP entirely onto the nitrogen atom, reducing it from a positive to neutral form.
In what is essentially the reverse of step two, the electrons push back in the opposite direction forming a new bond between the substrate carbon and another atom. (In the case of the decarboxylases, this creates a new carbon-hydrogen bond. In the case of transketolase, this attacks a new substrate molecule to form a new carbon-carbon bond.)
In what is essentially the reverse of step one, the TPP-substrate bond is broken, reforming the TPP ylid and the substrate carbonyl.

The TPP thiazolium ring can be deprotonated at C2 to become an ylid.
A full view of TPP. The arrow indicates the acidic proton.

References[edit]

^ ^a ^b Pavia, Donald L., Gary M. Lampman, George S. Kritz, Randall G. Engel (2006). Introduction to Organic Laboratory Techniques (4th Ed.). Thomson Brooks/Cole. pp. 304–5. ISBN 978-0-495-28069-9.
^ "PDBs for Biochemistry". Georgia State University. Retrieved 2009-02-07.
^ Voet, Donald; Judith Voet, Charlotte Pratt (2008). Fundamentals of Biochemistry. John Wiley & Sons Inc. p. 508. ISBN 978-0-470-12930-2. Cite uses deprecated parameters (help)

External links[edit]

UIC.edu

English Journal

An in vitro selection for small molecule triggered strand displacement and riboswitch activity.

Martini L, Meyer AJ, Ellefson JW, Milligan JN, Forlin M, Ellington AD, Mansy SS.
ACS synthetic biology.ACS Synth Biol.2015 May 15. [Epub ahead of print]
An in vitro selection method for ligand responsive RNA sensors was developed that exploited strand displacement reactions. The RNA library was based on the thiamine pyrophosphate (TPP) riboswitch, and RNA sequences capable of hybridizing to a target duplex DNA in a TPP regulated manner were identifi
PMID 25978303

Imaging metabolite dynamics in living cells using a Spinach-based riboswitch.

You M1, Litke JL1, Jaffrey SR2.
Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2015 May 11. pii: 201504354. [Epub ahead of print]
Riboswitches are natural ligand-sensing RNAs typically that are found in the 5' UTRs of mRNA. Numerous classes of riboswitches have been discovered, enabling mRNA to be regulated by diverse and physiologically important cellular metabolites and small molecules. Here we describe Spinach riboswitches,
PMID 25964329

Regulation of basal promoter activity of the human thiamine pyrophosphate transporter SLC44A4 in human intestinal epithelial cells.

Nabokina SM1, Ramos MB1, Valle JE1, Said HM2.
American journal of physiology. Cell physiology.Am J Physiol Cell Physiol.2015 May 1;308(9):C750-7. doi: 10.1152/ajpcell.00381.2014. Epub 2015 Feb 25.
Microbiota of the large intestine synthesize considerable amount of vitamin B1 in the form of thiamine pyrophosphate (TPP). There is a specific high-affinity regulated carrier-mediated uptake system for TPP in human colonocytes (product of the SLC44A4 gene). The mechanisms of regulation of SLC44A4 g
PMID 25715703

Japanese Journal

Early metabolic reactivation versus antioxidant therapy after a traumatic spinal cord injury in adult rats

TORRES Sergio,SALGADO-CEBALLOS Hermelinda,TORRES Jose Luis,OROZCO-SUAREZ Sandra,DIAZ-RUIZ Araceli,MARTINEZ Angelina,RIVERA-CRUZ Mario,RIOS Camilo,LARA Alicia,COLLADO Carlos,GUIZAR-SAHAGUN Gabriel
Neuropathology : official journal the Japanese Society of Neuropathology 30(1), 36-43, 2010-02-01
NAID 10029319860

偏性嫌気性スピロへータを含めた歯周ポケット内細菌の培養法の検討

梅田誠
日本歯周病学会会誌 29(1), 91-105, 1987-03-28
本研究は歯周病の臨床検査として偏性嫌気性スピロへ一タを含めた歯肉縁下プラークの細菌叢を検索する方法を確立するという目的で行った。被験者28名において歯周ポケット内細菌叢を検索し各培地・培養法の比較, 検討を行った。非選択培地としてはスチールウールジャー法を用いたEG寒天培地が適していることが分かった。また偏性嫌気性スピロヘータの培養については, プレートインボトル法を用いた10% Rumen液入り …
NAID 110003988931

Cardiocrome の心臓, 血管系および白血球減少症に対する作用

鶴田克彦
九州齒科學會雜誌 : Kyushu-Shika-Gakkai-zasshi 37(1), 114-134, 1983-02-25
… Cardiocrome is the activator of tissue respiration, which is the admixture consisted of cytochrome c, cocarboxylase and riboflavin phosphate. … It may be presumed that these actions of Cardiocrome is owing to both the reagents, cocarboxylase and riboflavin phosphate, contained in Cardiocrome. …
NAID 110003007286

Related Pictures

★リンクテーブル★

リンク元	「コカルボキシラーゼ」

「コカルボキシラーゼ」

Thiamine pyrophosphate
	IUPAC name 2-[3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-1,3-thiazol-3-ium-5-yl]ethyl phosphono hydrogen phosphate
	Other names Thiamine diphosphate
Identifiers
CAS number	154-87-0
PubChem	1132
ChemSpider	10670483
UNII	Q57971654Y
MeSH	Thiamine+pyrophosphate
Jmol-3D images	Image 1
	SMILES [Cl-].OP(=O)(O)OP(O)(O)=O.Cc2nc(N)c(C[n+]1csc(CCO)c1C)cn2 ;
	InChI InChI=1S/C12H17N4OS.ClH.H4O7P2/c1-8-11(3-4-17)18-7-16(8)6-10-5-14-9(2)15-12(10)13;;1-8(2,3)7-9(4,5)6/h5,7,17H,3-4,6H2,1-2H3,(H2,13,14,15);1H;(H2,1,2,3)(H2,4,5,6)/q+1;;/p-1 ; Key: NBSUTVXQOGUTJX-UHFFFAOYSA-M InChI=1/C12H17N4OS.ClH.H4O7P2/c1-8-11(3-4-17)18-7-16(8)6-10-5-14-9(2)15-12(10)13;;1-8(2,3)7-9(4,5)6/h5,7,17H,3-4,6H2,1-2H3,(H2,13,14,15);1H;(H2,1,2,3)(H2,4,5,6)/q+1;;/p-1; Key: NBSUTVXQOGUTJX-REWHXWOFAB ;
Properties
Molecular formula	C12H19N4O7P2S+
Molar mass	425.314382 g/mol
	Except where noted otherwise, data are given for materials in their standard state (at 25 °C (77 °F), 100 kPa)
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	Infobox references

　　[★]

英: cocarboxylase
同: チアミンピロリン酸 thiamine pyrophosphate TPP、チアミン二リン酸 thiamine diphosphate、ジホスホチアミン diphosphothiamine、アノイリンピロリン酸 aneurine pyrophosphate
商: アリチラーゼ、プロフィット
関: 活性チアミン誘導体、脚気

[Pavia-1] Pavia, Donald L., Gary M. Lampman, George S. Kritz, Randall G. Engel (2006). Introduction to Organic Laboratory Techniques (4th Ed.). Thomson Brooks/Cole. pp. 304–5. ISBN 978-0-495-28069-9.

[GSU-2] "PDBs for Biochemistry". Georgia State University. Retrieved 2009-02-07.

[Voet-3] Voet, Donald; Judith Voet, Charlotte Pratt (2008). Fundamentals of Biochemistry. John Wiley & Sons Inc. p. 508. ISBN 978-0-470-12930-2. Cite uses deprecated parameters (help)

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案内

cocarboxylase