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Record Information
Version3.6
Creation Date2005-11-16 15:48:42 UTC
Update Date2017-09-14 00:14:58 UTC
HMDB IDHMDB0001372
Secondary Accession Numbers
  • HMDB01372
Metabolite Identification
Common NameThiamine pyrophosphate
DescriptionThiamine pyrophosphate is the active form of thiamine, and it serves as a cofactor for several enzymes involved primarily in carbohydrate catabolism. The enzymes are important in the biosynthesis of a number of cell constituents, including neurotransmitters, and for the production of reducing equivalents used in oxidant stress defenses and in biosyntheses and for synthesis of pentoses used as nucleic acid precursors. The chemical structure of TPP is that of an aromatic methylaminopyrimidine ring, linked via a methylene bridge to a methylthiazolium ring with a pyrophosphate group attached to a hydroxyethyl side chain. In non-enzymatic model studies it has been demonstrated that the thiazolium ring can catalyse reactions which are similar to those of TPP-dependent enzymes but several orders of magnitude slower. Using infrared and NMR spectrophotometry it has been shown that the dissociation of the proton from C2 of the thiazolium ring is necessary for catalysis; the abstraction of the proton leads to the formation of a carbanion (ylid) with the potential for a nucleophilic attack on the carbonyl group of the substrate. In all TPP-dependent enzymes the abstraction of the proton from the C2 atom is the first step in catalysis, which is followed by a nucleophilic attack of this carbanion on the substrate. Subsequent cleavage of a C-C bond releases the first product with formation of a second carbanion (2-greek small letter alpha-carbanion or enamine). The formation of this 2-greek small letter alpha-carbanion is the second feature of TPP catalysis common to all TPP-dependent enzymes. Depending on the enzyme and the substrate(s), the reaction intermediates and products differ. Methyl-branched fatty acids, as phytanic acid, undergo peroxisomal beta-oxidation in which they are shortened by 1 carbon atom. This process includes four steps: activation, 2-hydroxylation, thiamine pyrophosphate dependent cleavage and aldehyde dehydrogenation. In the third step, 2-hydroxy-3-methylacyl-CoA is cleaved in the peroxisomal matrix by 2-hydroxyphytanoyl-CoA lyase (2-HPCL), which uses thiamine pyrophosphate (TPP) as cofactor. The thiamine pyrophosphate dependence of the third step is unique in peroxisomal mammalian enzymology. Human pathology due to a deficient alpha-oxidation is mostly linked to mutations in the gene coding for the second enzyme of the sequence, phytanoyl-CoA hydroxylase (EC 1.14.11.18). (PMID: 12694175 , 11899071 , 9924800 ).
Structure
Thumb
Synonyms
ValueSource
Thiamin diphosphateChEBI
Thiamin pyrophosphateChEBI
Thiamine diphosphateChEBI
THPPChEBI
TPPChEBI
Thiamin diphosphoric acidGenerator
Thiamine pyrophosphoric acidGenerator
Thiamin pyrophosphoric acidGenerator
Thiamine diphosphoric acidGenerator
Thaimine pyrophosphateHMDB
Thiamin-ppiHMDB
Thiamine-ppiHMDB
Thiamine-pyrophosphateHMDB
CocarboxylaseMeSH
BerolaseMeSH
Pyrophosphate, thiamineMeSH
Chemical FormulaC12H19N4O7P2S
Average Molecular Weight425.314
Monoisotopic Molecular Weight425.044967696
IUPAC Name3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-{[hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium
Traditional Namethiamin pyrophosphate
CAS Registry Number154-87-0
SMILES
CC1=C(CCO[P@](O)(=O)OP(O)(O)=O)SC=[N+]1CC1=CN=C(C)N=C1N
InChI Identifier
InChI=1S/C12H18N4O7P2S/c1-8-11(3-4-22-25(20,21)23-24(17,18)19)26-7-16(8)6-10-5-14-9(2)15-12(10)13/h5,7H,3-4,6H2,1-2H3,(H4-,13,14,15,17,18,19,20,21)/p+1
InChI KeyAYEKOFBPNLCAJY-UHFFFAOYSA-O
Chemical Taxonomy
DescriptionThis compound belongs to the class of chemical entities known as thiamine phosphates. These are thiamine derivatives in which the hydroxyl group of the ethanol moiety is substituted by a phosphate group.
KingdomChemical entities
Super ClassOrganic compounds
ClassOrganoheterocyclic compounds
Sub ClassDiazines
Direct ParentThiamine phosphates
Alternative Parents
Substituents
  • Thiamine-phosphate
  • Organic pyrophosphate
  • 4,5-disubstituted 1,3-thiazole
  • Monoalkyl phosphate
  • Hydropyrimidine
  • Organic phosphoric acid derivative
  • Phosphoric acid ester
  • Alkyl phosphate
  • Imidolactam
  • Thiazole
  • Azole
  • Heteroaromatic compound
  • Azacycle
  • Organic oxide
  • Organic nitrogen compound
  • Organopnictogen compound
  • Organooxygen compound
  • Organonitrogen compound
  • Organic oxygen compound
  • Hydrocarbon derivative
  • Organic cation
  • Aromatic heteromonocyclic compound
Molecular FrameworkAromatic heteromonocyclic compounds
External Descriptors
Ontology
StatusDetected and Quantified
Origin
  • Endogenous
Biofunction
  • Component of Thiamine metabolism
ApplicationNot Available
Cellular locations
  • Cytoplasm
  • Mitochondria
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
Water Solubility0.15 mg/mLALOGPS
logP-1.2ALOGPS
logP-5.8ChemAxon
logS-3.5ALOGPS
pKa (Strongest Acidic)1.78ChemAxon
pKa (Strongest Basic)5.53ChemAxon
Physiological Charge-1ChemAxon
Hydrogen Acceptor Count8ChemAxon
Hydrogen Donor Count4ChemAxon
Polar Surface Area168.97 Å2ChemAxon
Rotatable Bond Count8ChemAxon
Refractivity95.15 m3·mol-1ChemAxon
Polarizability36.96 Å3ChemAxon
Number of Rings2ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash Key
Predicted GC-MSPredicted GC-MS Spectrum - GC-MSNot Available
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-004i-0201900000-9ca110d3800e4ebfad43View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-00di-0900000000-dad8835a4b26b1df86c4View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-00di-2900000000-83b0eb52fe05e7097affView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 10V, Negativesplash10-00di-0000900000-538ee08c2fc9a905eaadView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 20V, Negativesplash10-0udi-0309000000-b196fd5684e86907d04eView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 30V, Negativesplash10-0udi-0409000000-088cf88d5056ce245770View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 40V, Negativesplash10-004i-9822000000-011b97ebb9fdcebffc93View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 50V, Negativesplash10-004i-9200000000-2ecd5ee7eb283c5cd990View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 10V, Positivesplash10-004i-0001900000-59ea8d394aed62700202View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 20V, Positivesplash10-00b9-0614900000-08f09a377f03019f4457View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 30V, Positivesplash10-00di-0911000000-de2b56b98b01c6409b09View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 40V, Positivesplash10-00di-0900000000-7d75ca5105912446e47bView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 50V, Positivesplash10-00di-2900000000-d632b8688f17a7a01de0View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , negativesplash10-00di-0000900000-538ee08c2fc9a905eaadView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , negativesplash10-0udi-0309000000-b196fd5684e86907d04eView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , negativesplash10-0udi-0409000000-088cf88d5056ce245770View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , negativesplash10-004i-9822000000-670f784e69ef56047333View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , negativesplash10-004i-9200000000-2ecd5ee7eb283c5cd990View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-004i-0001900000-59ea8d394aed62700202View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, NegativeNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, NegativeNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, NegativeNot Available
1D NMR1H NMR SpectrumNot Available
2D NMR[1H,13C] 2D NMR SpectrumNot Available
Biological Properties
Cellular Locations
  • Cytoplasm
  • Mitochondria
Biofluid Locations
  • Blood
  • Cerebrospinal Fluid (CSF)
Tissue Location
  • Brain
  • Erythrocyte
  • Fibroblasts
Pathways
2-Methyl-3-Hydroxybutryl CoA Dehydrogenase DeficiencyPw000061Pw000061 greyscalePw000061 simpleNot Available
2-aminoadipic 2-oxoadipic aciduriaPw000696Pw000696 greyscalePw000696 simpleNot Available
2-ketoglutarate dehydrogenase complex deficiencyPw000525Pw000525 greyscalePw000525 simpleNot Available
3-Hydroxy-3-Methylglutaryl-CoA Lyase DeficiencyPw000063Pw000063 greyscalePw000063 simpleNot Available
3-Methylcrotonyl Coa Carboxylase Deficiency Type IPw000065Pw000065 greyscalePw000065 simpleNot Available
Displaying entries 1 - 5 of 54 in total
Normal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
Cerebrospinal Fluid (CSF)Detected and Quantified0.0032 +/- 0.0022 uMAdult (>18 years old)BothNormal details
Abnormal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified0.034 (0-0.066) uMAdult (>18 years old)Not Specified
Cerebrocortical Degeneration
details
Cerebrospinal Fluid (CSF)Detected and Quantified0.0025 +/- 0.0017 uMAdult (>18 years old)BothAlzheimer's disease details
Associated Disorders and Diseases
Disease References
Alzheimer's disease
  1. Molina JA, Jimenez-Jimenez FJ, Hernanz A, Fernandez-Vivancos E, Medina S, de Bustos F, Gomez-Escalonilla C, Sayed Y: Cerebrospinal fluid levels of thiamine in patients with Alzheimer's disease. J Neural Transm (Vienna). 2002 Jul;109(7-8):1035-44. [PubMed:12111441 ]
Cerebrocortical degeneration
  1. Holtershinken M, Hohling A, Witte B, Scholz H: [Thiamine and its derivates in cattle blood measured by HPLC in healthy animals, in patients suffering from CCN and in their cohorts]. Dtsch Tierarztl Wochenschr. 2007 Jun;114(6):212-8. [PubMed:17642321 ]
Associated OMIM IDs
DrugBank IDNot Available
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDFDB022584
KNApSAcK IDNot Available
Chemspider ID1100
KEGG Compound IDC00068
BioCyc ID2-(alpha-lactyl)-thpp
BiGG ID33732
Wikipedia LinkThiamine pyrophosphate
NuGOwiki LinkHMDB0001372
METLIN ID2832
PubChem Compound1132
PDB IDTPP
ChEBI ID9532
References
Synthesis ReferenceZabrodskaya, S. V.; Oparin, D. A.; Ostrovskii, Yu. M. Selective synthesis of thiamine diphosphate. Zhurnal Obshchei Khimii (1989), 59(1), 226-7.
Material Safety Data Sheet (MSDS)Download (PDF)
General References
  1. Foulon V, Sniekers M, Huysmans E, Asselberghs S, Mahieu V, Mannaerts GP, Van Veldhoven PP, Casteels M: Breakdown of 2-hydroxylated straight chain fatty acids via peroxisomal 2-hydroxyphytanoyl-CoA lyase: a revised pathway for the alpha-oxidation of straight chain fatty acids. J Biol Chem. 2005 Mar 18;280(11):9802-12. Epub 2005 Jan 11. [PubMed:15644336 ]
  2. Singleton CK, Martin PR: Molecular mechanisms of thiamine utilization. Curr Mol Med. 2001 May;1(2):197-207. [PubMed:11899071 ]
  3. Molina JA, Jimenez-Jimenez FJ, Hernanz A, Fernandez-Vivancos E, Medina S, de Bustos F, Gomez-Escalonilla C, Sayed Y: Cerebrospinal fluid levels of thiamine in patients with Alzheimer's disease. J Neural Transm (Vienna). 2002 Jul;109(7-8):1035-44. [PubMed:12111441 ]
  4. Shimon I, Almog S, Vered Z, Seligmann H, Shefi M, Peleg E, Rosenthal T, Motro M, Halkin H, Ezra D: Improved left ventricular function after thiamine supplementation in patients with congestive heart failure receiving long-term furosemide therapy. Am J Med. 1995 May;98(5):485-90. [PubMed:7733128 ]
  5. Floridi A, Pupita M, Palmerini CA, Fini C, Alberti Fidanza A: Thiamine pyrophosphate determination in whole blood and erythrocytes by high performance liquid chromatography. Int J Vitam Nutr Res. 1984;54(2-3):165-71. [PubMed:6500839 ]
  6. Essama-Tjani JC, Guilland JC, Fuchs F, Lombard M, Richard D: Changes in thiamin, riboflavin, niacin, beta-carotene, vitamins, C, A, D and E status of French Elderly Subjects during the first year of institutionalization. Int J Vitam Nutr Res. 2000 Mar;70(2):54-64. [PubMed:10804457 ]
  7. Warnock LG: The measurement of erythrocyte thiamin pyrophosphate by high-performance liquid chromatography. Anal Biochem. 1982 Nov 1;126(2):394-7. [PubMed:7158773 ]
  8. Lynch PL, Trimble ER, Young IS: High-performance liquid chromatographic determination of thiamine diphosphate in erythrocytes using internal standard methodology. J Chromatogr B Biomed Sci Appl. 1997 Nov 7;701(1):120-3. [PubMed:9389346 ]
  9. Naito E, Ito M, Yokota I, Saijo T, Ogawa Y, Kuroda Y: Diagnosis and molecular analysis of three male patients with thiamine-responsive pyruvate dehydrogenase complex deficiency. J Neurol Sci. 2002 Sep 15;201(1-2):33-7. [PubMed:12163191 ]
  10. Baines M: Improved high performance liquid chromatographic determination of thiamin diphosphate in erythrocytes. Clin Chim Acta. 1985 Nov 29;153(1):43-8. [PubMed:4075519 ]
  11. Duffy P, Morris H, Neilson G: Thiamin status of a Melanesian population. Am J Clin Nutr. 1981 Aug;34(8):1584-92. [PubMed:7270482 ]
  12. Kjosen B, Seim SH: The transketolase assay of thiamine in some diseases. Am J Clin Nutr. 1977 Oct;30(10):1591-6. [PubMed:910736 ]
  13. Winston AP, Jamieson CP, Madira W, Gatward NM, Palmer RL: Prevalence of thiamin deficiency in anorexia nervosa. Int J Eat Disord. 2000 Dec;28(4):451-4. [PubMed:11054793 ]
  14. Levy S, Herve C, Delacoux E, Erlinger S: Thiamine deficiency in hepatitis C virus and alcohol-related liver diseases. Dig Dis Sci. 2002 Mar;47(3):543-8. [PubMed:11911339 ]
  15. Talwar D, Davidson H, Cooney J, St JO'Reilly D: Vitamin B(1) status assessed by direct measurement of thiamin pyrophosphate in erythrocytes or whole blood by HPLC: comparison with erythrocyte transketolase activation assay. Clin Chem. 2000 May;46(5):704-10. [PubMed:10794754 ]
  16. Fidanza F, Simonetti MS, Floridi A, Codini M, Fidanza R: Comparison of methods for thiamin and riboflavin nutriture in man. Int J Vitam Nutr Res. 1989;59(1):40-7. [PubMed:2722424 ]
  17. Tate JR, Nixon PF: Measurement of Michaelis constant for human erythrocyte transketolase and thiamin diphosphate. Anal Biochem. 1987 Jan;160(1):78-87. [PubMed:3565758 ]
  18. Frank T, Bitsch R, Maiwald J, Stein G: High thiamine diphosphate concentrations in erythrocytes can be achieved in dialysis patients by oral administration of benfontiamine. Eur J Clin Pharmacol. 2000 Jun;56(3):251-7. [PubMed:10952481 ]
  19. Lavoie J, Butterworth RF: Reduced activities of thiamine-dependent enzymes in brains of alcoholics in the absence of Wernicke's encephalopathy. Alcohol Clin Exp Res. 1995 Aug;19(4):1073-7. [PubMed:7485819 ]
  20. Casteels M, Foulon V, Mannaerts GP, Van Veldhoven PP: Alpha-oxidation of 3-methyl-substituted fatty acids and its thiamine dependence. Eur J Biochem. 2003 Apr;270(8):1619-27. [PubMed:12694175 ]
  21. Schenk G, Duggleby RG, Nixon PF: Properties and functions of the thiamin diphosphate dependent enzyme transketolase. Int J Biochem Cell Biol. 1998 Dec;30(12):1297-318. [PubMed:9924800 ]

Enzymes

General function:
Involved in catalytic activity
Specific function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Gene Name:
PDHB
Uniprot ID:
P11177
Molecular weight:
39233.1
Reactions
Pyruvic acid + Thiamine pyrophosphate → 2-(a-Hydroxyethyl)thiamine diphosphate + Carbon dioxidedetails
2-(a-Hydroxyethyl)thiamine diphosphate + Enzyme N6-(lipoyl)lysine → [Dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + Thiamine pyrophosphatedetails
General function:
Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Specific function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Gene Name:
PDHA1
Uniprot ID:
P08559
Molecular weight:
43295.255
Reactions
Pyruvic acid + Thiamine pyrophosphate → 2-(a-Hydroxyethyl)thiamine diphosphate + Carbon dioxidedetails
2-(a-Hydroxyethyl)thiamine diphosphate + Enzyme N6-(lipoyl)lysine → [Dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + Thiamine pyrophosphatedetails
General function:
Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Specific function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Gene Name:
PDHA2
Uniprot ID:
P29803
Molecular weight:
42932.855
Reactions
Pyruvic acid + Thiamine pyrophosphate → 2-(a-Hydroxyethyl)thiamine diphosphate + Carbon dioxidedetails
2-(a-Hydroxyethyl)thiamine diphosphate + Enzyme N6-(lipoyl)lysine → [Dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + Thiamine pyrophosphatedetails
General function:
Involved in catalytic activity
Specific function:
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Gene Name:
BCKDHB
Uniprot ID:
P21953
Molecular weight:
43122.065
Reactions
Alpha-ketoisovaleric acid + Thiamine pyrophosphate → 2-Methyl-1-hydroxypropyl-ThPP + Carbon dioxidedetails
2-Methyl-1-hydroxypropyl-ThPP + Enzyme N6-(lipoyl)lysine → [Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + Thiamine pyrophosphatedetails
Ketoleucine + Thiamine pyrophosphate → 3-Methyl-1-hydroxybutyl-ThPP + Carbon dioxidedetails
3-Methyl-1-hydroxybutyl-ThPP + Enzyme N6-(lipoyl)lysine → [Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(3-methylbutanoyl)dihydrolipoyllysine + Thiamine pyrophosphatedetails
3-Methyl-2-oxovaleric acid + Thiamine pyrophosphate → 2-Methyl-1-hydroxybutyl-ThPP + Carbon dioxidedetails
2-Methyl-1-hydroxybutyl-ThPP + Enzyme N6-(lipoyl)lysine → [Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + Thiamine pyrophosphatedetails
General function:
Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Specific function:
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Gene Name:
BCKDHA
Uniprot ID:
P12694
Molecular weight:
50470.58
Reactions
Alpha-ketoisovaleric acid + Thiamine pyrophosphate → 2-Methyl-1-hydroxypropyl-ThPP + Carbon dioxidedetails
2-Methyl-1-hydroxypropyl-ThPP + Enzyme N6-(lipoyl)lysine → [Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + Thiamine pyrophosphatedetails
Ketoleucine + Thiamine pyrophosphate → 3-Methyl-1-hydroxybutyl-ThPP + Carbon dioxidedetails
3-Methyl-1-hydroxybutyl-ThPP + Enzyme N6-(lipoyl)lysine → [Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(3-methylbutanoyl)dihydrolipoyllysine + Thiamine pyrophosphatedetails
3-Methyl-2-oxovaleric acid + Thiamine pyrophosphate → 2-Methyl-1-hydroxybutyl-ThPP + Carbon dioxidedetails
2-Methyl-1-hydroxybutyl-ThPP + Enzyme N6-(lipoyl)lysine → [Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + Thiamine pyrophosphatedetails
General function:
Involved in oxoglutarate dehydrogenase (succinyl-transferring) activity
Specific function:
The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
Gene Name:
OGDH
Uniprot ID:
Q02218
Molecular weight:
48179.59
Reactions
Oxoglutaric acid + Thiamine pyrophosphate → 3-Carboxy-1-hydroxypropylthiamine diphosphate + Carbon dioxidedetails
3-Carboxy-1-hydroxypropylthiamine diphosphate + Enzyme N6-(lipoyl)lysine → [Dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + Thiamine pyrophosphatedetails
General function:
Involved in thiamin diphosphokinase activity
Specific function:
Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. Can also catalyze the phosphorylation of pyrithiamine to pyrithiamine pyrophosphate.
Gene Name:
TPK1
Uniprot ID:
Q9H3S4
Molecular weight:
27265.05
Reactions
Adenosine triphosphate + Thiamine → Adenosine monophosphate + Thiamine pyrophosphatedetails
Adenosine triphosphate + Thiamine pyrophosphate → ADP + Thiamine triphosphatedetails
General function:
Involved in catalytic activity
Specific function:
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate (By similarity).
Gene Name:
TKTL1
Uniprot ID:
P51854
Molecular weight:
59302.195
General function:
Involved in catalytic activity
Specific function:
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Gene Name:
TKT
Uniprot ID:
P29401
Molecular weight:
67876.95
General function:
Involved in hydrolase activity
Specific function:
Uridine diphosphatase (UDPase) that promotes protein N-glycosylation and ATP level regulation. UDP hydrolysis promotes protein N-glycosylation and folding in the endoplasmic reticulum, as well as elevated ATP consumption in the cytosol via an ATP hydrolysis cycle. Together with CMPK1 and AK1, constitutes an ATP hydrolysis cycle that converts ATP to AMP and results in a compensatory increase in aerobic glycolysis. Also hydrolyzes GDP and IDP but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. Plays a key role in the AKT1-PTEN signaling pathway by promoting glycolysis in proliferating cells in response to phosphoinositide 3-kinase (PI3K) signaling (By similarity).
Gene Name:
ENTPD5
Uniprot ID:
O75356
Molecular weight:
47516.985
General function:
Involved in adenylate cyclase activity
Specific function:
Hydrolase highly specific for thiamine triphosphate (ThTP).
Gene Name:
THTPA
Uniprot ID:
Q9BU02
Molecular weight:
25565.685
Reactions
Thiamine triphosphate + Water → Thiamine pyrophosphate + Phosphoric aciddetails
General function:
Involved in catalytic activity
Specific function:
Plays an essential role in total transketolase activity and cell proliferation in cancer cells; after transfection with anti-TKTL1 siRNA, total transketolase activity dramatically decreases and proliferation was significantly inhibited in cancer cells. Plays a pivotal role in carcinogenesis.
Gene Name:
TKTL2
Uniprot ID:
Q9H0I9
Molecular weight:
67876.625
General function:
Involved in magnesium ion binding
Specific function:
Not Available
Gene Name:
ILVBL
Uniprot ID:
A1L0T0
Molecular weight:
67867.2
General function:
Involved in magnesium ion binding
Specific function:
Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde.
Gene Name:
HACL1
Uniprot ID:
Q9UJ83
Molecular weight:
63728.095
General function:
Involved in oxoglutarate dehydrogenase (succinyl-transferring) activity
Specific function:
The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Gene Name:
DHTKD1
Uniprot ID:
Q96HY7
Molecular weight:
103042.15
General function:
Involved in oxoglutarate dehydrogenase (succinyl-transferring) activity
Specific function:
Not Available
Gene Name:
OGDHL
Uniprot ID:
Q9ULD0
Molecular weight:
Not Available
Reactions
Oxoglutaric acid + Thiamine pyrophosphate → 3-Carboxy-1-hydroxypropylthiamine diphosphate + Carbon dioxidedetails
3-Carboxy-1-hydroxypropylthiamine diphosphate + Enzyme N6-(lipoyl)lysine → [Dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + Thiamine pyrophosphatedetails
General function:
Involved in nucleotide binding
Specific function:
Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency.
Gene Name:
NTPCR
Uniprot ID:
Q9BSD7
Molecular weight:
20712.935
Reactions
Thiamine pyrophosphate + Water → Thiamine monophosphate + Phosphoric aciddetails