チアミン二リン酸 TDP, thiamine pyrophosphate TPP
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/09/20 19:34:11」(JST)
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Thiamine pyrophosphate
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| Names |
| IUPAC name
2-[3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-1,3-thiazol-3-ium-5-yl]ethyl phosphono hydrogen phosphate
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| Other names
Thiamine diphosphate
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| Identifiers |
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CAS Registry Number
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154-87-0 Y |
| ChemSpider |
10670483 Y |
InChI
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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 Y
Key: NBSUTVXQOGUTJX-UHFFFAOYSA-M Y
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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
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| Jmol-3D images |
Image |
| MeSH |
Thiamine+pyrophosphate |
| PubChem |
1132 |
SMILES
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[Cl-].OP(=O)(O)OP(O)(O)=O.Cc2nc(N)c(C[n+]1csc(CCO)c1C)cn2
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| UNII |
Q57971654Y Y |
| Properties |
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Chemical formula
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C12H19N4O7P2S+ |
| Molar mass |
425.314382 g/mol |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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| Y verify (what is: Y/N?) |
| Infobox references |
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Thiamine pyrophosphate (TPP or ThPP), or thiamine diphosphate (ThDP), or cocarboxylase[1] is a thiamine (vitamin B1) derivative which is produced by the enzyme thiamine diphosphokinase. 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.[2]
TPP works as a coenzyme in many enzymatic reactions, such as:
- Pyruvate dehydrogenase complex[3]
- Pyruvate decarboxylase in ethanol fermentation
- Alpha-ketoglutarate dehydrogenase complex
- Branched-chain amino acid dehydrogenase complex
- 2-hydroxyphytanoyl-CoA lyase
- Transketolase
Contents
- 1 Chemistry
- 2 Reaction mechanisms
- 3 References
- 4 External links
Chemistry
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".[2][4]
Reaction mechanisms
In several reactions, including that of pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase, and transketolase, TPP catalyses the reversible decarboxylation reaction (aka 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.
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The TPP thiazolium ring can be deprotonated at C2 to become an ylid.
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A full view of TPP. The arrow indicates the acidic proton.
References
- ^ Pietrzak I (1995). "[Vitamin disturbances in chronic renal insufficiency. I. Water soluble vitamins]". Przegla̧D Lekarski (in Polish) 52 (10): 522–5. PMID 8834846.
- ^ 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.
External links
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Enzyme cofactors
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| Active forms |
| vitamins |
- TPP / ThDP (B1)
- FMN, FAD (B2)
- NAD+, NADH, NADP+, NADPH (B3)
- Coenzyme A (B5)
- PLP / P5P (B6)
- Biotin (B7)
- THFA / H4FA, DHFA / H2FA, MTHF (B9)
- AdoCbl, MeCbl (B12)
- Ascorbic acid (C)
- Phylloquinone (K1), Menaquinone (K2)
- Coenzyme F420
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| non-vitamins |
- ATP
- CTP
- SAMe
- PAPS
- GSH
- Coenzyme B
- Cofactor F430
- Coenzyme M
- Coenzyme Q
- Heme / Haem (A, B, C, O)
- Lipoic Acid
- Methanofuran
- Molybdopterin/Molybdenum cofactor
- PQQ
- THB / BH4
- THMPT / H4MPT
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| minerals |
- Ca2+
- Cu2+
- Fe2+, Fe3+
- Mg2+
- Mn2+
- Mo
- Ni2+
- Zn2+
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| Base forms |
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Index of nutrition
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| Description |
- Vitamins
- Cofactors
- Metal metabolism
- Fats
- metabolism
- intermediates
- lipoproteins
- Sugars
- Glycolysis
- Glycogenesis and glycogenolysis
- Fructose and galactose
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| Disease |
- Vitamins
- Carbohydrate
- Lipid
- Metals
- Other
- Symptoms and signs
- Tests
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| Treatment |
- Drugs
- Vitamins
- Mineral supplements
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UpToDate Contents
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English Journal
- Joint effects of gamma radiation and cadmium on subcellular-, individual- and population-level endpoints of the green microalga Raphidocelis subcapitata.
- Bradshaw C, Meseh DA, Alasawi H, Qiang M, Snoeijs-Leijonmalm P, Nascimento FJA.
- Aquatic toxicology (Amsterdam, Netherlands). 2019 Jun;211()217-226.
- Interpreting and predicting the combined effects of toxicants in the environment is an important challenge in ecotoxicology. How such effects are connected across different levels of biological organisation is an additional matter of uncertainty. Such knowledge gaps are particularly prominent with r
- PMID 31035029
- Navigating within thiamine diphosphate-dependent decarboxylases: sequences, structures, functional positions, and binding sites.
- Buchholz PCF, Ferrario V, Pohl M, Gardossi L, Pleiss J.
- Proteins. 2019 May;().
- Thiamine diphosphate-dependent decarboxylases catalyze both cleavage and formation of C-C-bonds in various reactions, which have been assigned to different homologous sequence families. This work compares 53 ThDP-dependent decarboxylases with known crystal structures. Both sequence and structural in
- PMID 31070804
- Characterisation of thiamine diphosphate-dependent 4-hydroxybenzoylformate decarboxylase enzymes from Rhodococcus jostii RHA1 and Pseudomonas fluorescens Pf-5 involved in degradation of aryl-C2 lignin degradation fragments.
- Wei Z, Wilkinson RC, Rashid GMM, Brown D, Fülöp V, Bugg TDH.
- Biochemistry. 2019 Apr;().
- A thiamine diphosphate-dependent enzyme annotated as a benzoylformate decarboxylase is encoded in gene cluster ro02984-ro02986 in Rhodococcus jostii RHA1 previously shown to generate vanillin and 4-hydroxybenzaldehyde from lignin oxidation, and a closely related gene cluster is also found in the gen
- PMID 30946572
Japanese Journal
- Determination of thiamin diphosphate in whole blood samples by high-performance liquid chromatography-A method suitable for pediatric diagnostics
- KORNER Robert Walter,VIERZIG Anne,ROTH Bernhard,MULLER Carsten
- Journal of chromatography. B, Analytical technologies in the biomedical and life sciences 877(20), 1882-1886, 2009-07-01
- NAID 10028019306
- Cooperation of Divalent Ions and Thiamin Diphosphate in Regulation of the Function of Pig Heart Pyruvate Dehydrogenase Complex
- CZERNIECKI Jan,CZYGIER Maria
- Journal of nutritional science and vitaminology 47(6), 385-386, 2001-12-01
- NAID 10013010453
Related Links
- thiamin diphosphate | C12H18N4O7P2S | CID 5431 - structure, chemical names, physical and chemical properties, classification, patents, literature, biological activities, safety/hazards/toxicity information, supplier lists, and more. ... ...
- The role of thiamin diphosphate (ThDP) as a cofactor for enzymes has been known for many decades. This minireview covers the progress made in understanding the catalytic mechanism of ThDP-dependent enzymes through the use ...
★リンクテーブル★
[★]
- 英
- thiamin diphosphate,TDP, thiamine pyrophosphate, TPP
- 関
- ビタミンB1 = チアミン
- ピルビン酸デヒドロゲナーゼ、ビタミンB1、チアミン thiamin
- コカルボキシラーゼ
[show details]
[★]
[★]
チアミン二リン酸 TDP, thiamin diphosphate, TPP
[★]
二リン酸エステル、二リン酸塩、二リン酸
- 関
- bisphosphate、diphosphoric acid、pyrophosphate
[★]
ビタミンB1、チアミン, thiamine