Record Information
Version2.0
Creation Date2012-05-31 13:51:11 -0600
Update Date2015-09-13 12:56:11 -0600
Secondary Accession Numbers
  • ECMDB01372
Identification
Name:Thiamine pyrophosphate
Description:Thiamine pyrophosphate (TPP) 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 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. (PMID: 12694175, 11899071, 9924800)
Structure
Thumb
Synonyms:
  • TDP
  • Thaimine pyrophosphate
  • Thaimine pyrophosphoric acid
  • Thiamin diphosphate
  • Thiamin diphosphoric acid
  • Thiamin pyrophosphate
  • Thiamin pyrophosphoric acid
  • Thiamin-PPi
  • Thiamine diphosphate
  • Thiamine diphosphoric acid
  • Thiamine pyrophosphate
  • Thiamine pyrophosphoric acid
  • Thiamine-PPi
  • Thiamine-pyrophosphate
  • Thiamine-pyrophosphoric acid
  • ThiamineDP
  • ThPP
  • TPP
Chemical Formula:C12H19N4O7P2S
Weight:Average: 425.314
Monoisotopic: 425.044967696
InChI Key:AYEKOFBPNLCAJY-UHFFFAOYSA-O
InChI: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
CAS number:154-87-0
IUPAC Name:3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-{[hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium
Traditional IUPAC Name:thiamin pyrophosphate
SMILES:CC1=C(CCO[P@](O)(=O)OP(O)(O)=O)SC=[N+]1CC1=CN=C(C)N=C1N
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
Physical Properties
State:Solid
Charge:-1
Melting point:Not Available
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility0.152 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
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
Adenosine triphosphate + Thiamine monophosphate <> ADP + Thiamine pyrophosphate
Water + Thiamine pyrophosphate > Hydrogen ion + Phosphate + Thiamine monophosphate
Pyruvic acid + Thiamine pyrophosphate <> 2-(a-Hydroxyethyl)thiamine diphosphate + Carbon dioxide
Adenosine triphosphate + Thiamine monophosphate <> ADP + Thiamine pyrophosphate
alpha-Ketoglutarate + Thiamine pyrophosphate <> 3-carboxy-1-hydroxypropylthiamine diphosphate + Carbon dioxide
2-Acetolactate + Thiamine pyrophosphate <> 2-(a-Hydroxyethyl)thiamine diphosphate + Pyruvic acid
2-(a-Hydroxyethyl)thiamine diphosphate + Enzyme N6-(lipoyl)lysine <> [Dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + Thiamine pyrophosphate
3-carboxy-1-hydroxypropylthiamine diphosphate + Enzyme N6-(lipoyl)lysine <> [Dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + Thiamine pyrophosphate
(S)-2-Acetolactate + Thiamine pyrophosphate <> 2-(a-Hydroxyethyl)thiamine diphosphate + Pyruvic acid
2-Ketobutyric acid + 2-(a-Hydroxyethyl)thiamine diphosphate <> 2-Aceto-2-hydroxy-butyrate + Thiamine pyrophosphate
Thiamine pyrophosphate + Water > Hydrogen ion + Thiamine monophosphate + Phosphate
2-(a-Hydroxyethyl)thiamine diphosphate + Pyruvate-dehydrogenase-lipoate > Thiamine pyrophosphate + Pyruvate-dehydrogenase-acetylDHlipoyl
Hydrogen ion + Pyruvic acid + Thiamine pyrophosphate > 2-(a-Hydroxyethyl)thiamine diphosphate + Carbon dioxide
Hydrogen ion + Thiamine pyrophosphate + ADP <> adenosine thiamine triphosphate + Phosphate
Thiamine monophosphate + Adenosine triphosphate > Thiamine pyrophosphate + ADP
Adenosine triphosphate + Thiamine monophosphate > ADP + Thiamine pyrophosphate
TDP-Fuc4NAc + Und-PP-GlcNAc-ManNAcA > Thiamine pyrophosphate + Und-PP-GlcNAc-ManNAcA-Fuc4NAc
Thiamine monophosphate + Adenosine triphosphate + Thiamine monophosphate > Thiamine pyrophosphate + Adenosine diphosphate + ADP
Adenosine triphosphate + Thiamine monophosphate > ADP + Thiamine pyrophosphate
SMPDB Pathways:
Thiamin diphosphate biosynthesisPW002028 Pw002028Pw002028 greyscalePw002028 simple
Vitamin B1/ThiaminePW000892 Pw000892Pw000892 greyscalePw000892 simple
pyruvate to cytochrome bd terminal oxidase electron transferPW002087 Pw002087Pw002087 greyscalePw002087 simple
KEGG Pathways:
EcoCyc Pathways:
  • thiamin diphosphate biosynthesis I (E. coli) PWY-6894
Concentrations
Not Available
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
GC-MSGC-MS Spectrum - GC-MSsplash10-002b-9734000000-83738512818790cf1cc5View in MoNA
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, Positivesplash10-004i-0100900000-2d5d6c77c0c7e2d2d28aView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0aba-8146900000-e4efbc495cf0eb380395View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0a4j-4911100000-7e4a6eda3f297e8051b7View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-00di-0000900000-08198f6dfeaa404b8b0fView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-001i-9100200000-2d9e7e5d87267ce83dccView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-004j-9200000000-a470e5de9f124c159e0eView in MoNA
1D NMR1H NMR SpectrumNot Available
2D NMR[1H,13C] 2D NMR SpectrumNot Available
References
References:
  • 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
  • Casteels, M., Foulon, V., Mannaerts, G. P., Van Veldhoven, P. P. (2003). "Alpha-oxidation of 3-methyl-substituted fatty acids and its thiamine dependence." Eur J Biochem 270:1619-1627. Pubmed: 12694175
  • Duffy P, Morris H, Neilson G: Thiamin status of a Melanesian population. Am J Clin Nutr. 1981 Aug;34(8):1584-92. Pubmed: 7270482
  • 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
  • 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
  • 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
  • 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
  • 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
  • Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
  • Kjosen B, Seim SH: The transketolase assay of thiamine in some diseases. Am J Clin Nutr. 1977 Oct;30(10):1591-6. Pubmed: 910736
  • 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
  • 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
  • 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
  • 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. 2002 Jul;109(7-8):1035-44. Pubmed: 12111441
  • 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
  • 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
  • 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
  • Singleton CK, Martin PR: Molecular mechanisms of thiamine utilization. Curr Mol Med. 2001 May;1(2):197-207. Pubmed: 11899071
  • 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
  • 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
  • van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. Pubmed: 17765195
  • Warnock LG: The measurement of erythrocyte thiamin pyrophosphate by high-performance liquid chromatography. Anal Biochem. 1982 Nov 1;126(2):394-7. Pubmed: 7158773
  • 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
Synthesis Reference:Zabrodskaya, 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)
External Links:
ResourceLink
CHEBI ID9532
HMDB IDHMDB01372
Pubchem Compound ID1132
Kegg IDC00068
ChemSpider ID1100
WikipediaThiamine pyrophosphate
BioCyc IDTHIAMINE-PYROPHOSPHATE
EcoCyc IDTHIAMINE-PYROPHOSPHATE
Ligand ExpoTPP

Enzymes

General function:
Involved in magnesium ion binding
Specific function:
2 pyruvate = 2-acetolactate + CO(2)
Gene Name:
ilvI
Uniprot ID:
P00893
Molecular weight:
62984
Reactions
2 pyruvate = 2-acetolactate + CO(2).
General function:
Involved in acetolactate synthase activity
Specific function:
2 pyruvate = 2-acetolactate + CO(2)
Gene Name:
ilvH
Uniprot ID:
P00894
Molecular weight:
17977
Reactions
2 pyruvate = 2-acetolactate + CO(2).
General function:
Involved in magnesium ion binding
Specific function:
2 pyruvate = 2-acetolactate + CO(2)
Gene Name:
ilvB
Uniprot ID:
P08142
Molecular weight:
60440
Reactions
2 pyruvate = 2-acetolactate + CO(2).
General function:
Involved in amino acid binding
Specific function:
2 pyruvate = 2-acetolactate + CO(2)
Gene Name:
ilvN
Uniprot ID:
P0ADF8
Molecular weight:
11106
Reactions
2 pyruvate = 2-acetolactate + CO(2).
General function:
Involved in acetolactate synthase activity
Specific function:
2 pyruvate = 2-acetolactate + CO(2)
Gene Name:
ilvM
Uniprot ID:
P0ADG1
Molecular weight:
9703
Reactions
2 pyruvate = 2-acetolactate + CO(2).
General function:
Involved in hydrolase activity
Specific function:
Catalyzes the hydrolysis of 4-amino-2-methyl-5- hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2- methyl-5-hydroxymethylpyrimidine phosphate (HMP-P), and hydrolysis of thiamine pyrophosphate (TPP) to thiamine monophosphate (TMP). Can hydrolyze other substrates such as MeO-HMP-PP, CF(3)-HMP-PP and MeO-TPP. Is also a non-specific nucleoside tri- and diphosphatase that releases inorganic orthophosphate
Gene Name:
nudJ
Uniprot ID:
P0AEI6
Molecular weight:
17433
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:
sucA
Uniprot ID:
P0AFG3
Molecular weight:
105061
Reactions
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
General function:
Involved in oxidoreductase activity
Specific function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3)
Gene Name:
aceE
Uniprot ID:
P0AFG8
Molecular weight:
99668
Reactions
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
General function:
Involved in catalytic activity
Specific function:
ATP + thiamine phosphate = ADP + thiamine diphosphate
Gene Name:
thiL
Uniprot ID:
P0AGG0
Molecular weight:
35070
Reactions
ATP + thiamine phosphate = ADP + thiamine diphosphate.
General function:
Involved in fucosyltransferase activity
Specific function:
Catalyzes the synthesis of Und-PP-GlcNAc-ManNAcA-Fuc4NAc (Lipid III), the third lipid-linked intermediate involved in ECA synthesis
Gene Name:
wecF
Uniprot ID:
P56258
Molecular weight:
40639
Reactions
TDP-Fuc4NAc + Und-PP-GlcNAc-ManNAcA = TDP + Und-PP-GlcNAc-ManNAcA-Fuc4NAc.