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Human Metabolome Database Version 2.5

 

Showing metabocard for Lipoic acid (HMDB01451)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:50
Accession Number HMDB01451
Secondary Accession Numbers Not Available
Common Name Lipoic acid
Description A vitamin-like antioxidant that acts as a free-radical scavenger. Alpha-lipoic acid is also known as thioctic acid. It is a naturally occurring compound that is synthesized by both plants and animals. Lipoic acid contains two thiol groups which may be either oxidized or reduced. The reduced form is known as dihydrolipoic acid (DHLA). Lipoic acid (Delta E= -0.288) is therefore capable of thiol-disulfide exchange, giving it antioxidant activity. Lipoate is a critical cofactor for aerobic metabolism, participating in the transfer of acyl or methylamine groups via the 2-Oxoacid dehydrogenase (2-OADH) or alpha-ketoglutarate dehydrogenase complex. This enzyme catalyzes the conversion of alpha-ketoglutarate to succinyl CoA. This activity results in the catabolism of the branched chain amino acids (leucine, isoleucine and valine). Lipoic acid also participates in the glycine cleavage system(GCV). The glycine cleavage system is a multi-enzyme complex that catalyzes the oxidation of glycine to form 5,10 methylene tetrahydrofolate, an important cofactor in nucleic acid synthesis. Since Lipoic acid is an essential cofactor for many enzyme complexes, it is essential for aerobic life as we know it. This system is used by many organisms and plays a crucial role in the photosynthetic carbon cycle. Lipoic acid was first postulated to be an effective antioxidant when it was found it prevented vitamin C and vitamin E deficiency. It is able to scavenge reactive oxygen species and reduce other metabolites, such as glutathione or vitamins, maintaining a healthy cellular redox state. Lipoic acid has been shown in cell culture experiments to increase cellular uptake of glucose by recruiting the glucose transporter GLUT4 to the cell membrane, suggesting its use in diabetes. Studies of rat aging have suggested that the use of L-carnitine and lipoic acid results in improved memory performance and delayed structural mitochondrial decay. As a result, it may be helpful for people with Alzheimer's disease or Parkinson's disease. -- Wikipedia
Synonyms
  1. (+)-alpha-Lipoate
  2. (+)-alpha-Lipoic acid
  3. (+-)-1,2-Dithiolane-3-pentanoate
  4. (+-)-1,2-Dithiolane-3-pentanoic acid
  5. (+-)-1,2-Dithiolane-3-valerate
  6. (+-)-1,2-Dithiolane-3-valeric acid
  7. (R)-1,2-Dithiolane-3-pentanoate
  8. (R)-1,2-Dithiolane-3-pentanoic acid
  9. (RS)-Lipoate
  10. (RS)-Lipoic acid
  11. (RS)-alpha-Lipoate
  12. (RS)-alpha-Lipoic acid
  13. 1,2-Dithiolane-3-pentanoate
  14. 1,2-Dithiolane-3-pentanoic acid
  15. 1,2-Dithiolane-3-valerate
  16. 1,2-Dithiolane-3-valeric acid
  17. 1,2-Dithiolane-3R-pentanoate
  18. 1,2-Dithiolane-3R-pentanoic acid
  19. 5-(1,2-Dithiolan-3-yl)pentanoate
  20. 5-(1,2-Dithiolan-3-yl)pentanoic acid
  21. 5-(1,2-Dithiolan-3-yl)valerate
  22. 5-(1,2-Dithiolan-3-yl)valeric acid
  23. 5-(Dithiolan-3-yl)valerate
  24. 5-(Dithiolan-3-yl)valeric acid
  25. 5-[3-(1,2-dithiolanyl)]pentanoate
  26. 5-[3-(1,2-dithiolanyl)]pentanoic acid
  27. 6,8-Dithiooctanoate
  28. 6,8-Dithiooctanoic acid
  29. 6,8-Thioctate
  30. 6,8-Thioctic acid
  31. 6,8-Thiotate
  32. 6,8-Thiotic acid
  33. 6-Thioctate
  34. 6-Thioctic acid
  35. 6-Thiotate
  36. 6-Thiotic acid
  37. Acetate-replacing factor
  38. Biletan
  39. DL-1,2-Dithiolane 3-valerate
  40. DL-1,2-Dithiolane 3-valeric acid
  41. DL-6,8-Dithiooctanoate
  42. DL-6,8-Dithiooctanoic acid
  43. DL-6,8-Thioctate
  44. DL-6,8-Thioctic acid
  45. DL-6-Thioctate
  46. DL-6-Thioctic acid
  47. DL-Thioctic acid > 98%
  48. DL-alpha-Lipoate
  49. DL-alpha-Lipoic acid
  50. Heparlipon
  51. Lip
  52. Lipoate
  53. Lipoic acid
  54. Liposan
  55. Lipothion
  56. Protogen A
  57. Pyruvate oxidation factor
  58. R-Lipoate
  59. R-Lipoic acid
  60. Rac-lipoate
  61. Thioctacid
  62. Thioctan
  63. Thioctate
  64. Thioctic acid
  65. Thioctic acid d-form
  66. Thioctic acid dl-form
  67. Thioctidase
  68. Thioctsan
  69. Thioktsaeure
  70. Thiooctanoate
  71. Thiooctanoic acid
  72. Tioctacid
  73. Tioctan
  74. Tioctidasi
  75. Tioctidasi acetate replacing factor
  76. acetate replacing factor
  77. alpha Lipoate
  78. alpha Lipoic acid
  79. alpha-Lipoate
  80. alpha-Lipoic acid
  81. alpha-Liponate
  82. alpha-Liponic acid
  83. alpha-Liponsaeure
  84. delta-[3-(1,2-dithiacyclopentyl)]pentanoate
  85. delta-[3-(1,2-dithiacyclopentyl)]pentanoic acid
  86. dl-Lipoate
  87. dl-Lipoic acid
  88. dl-Thioctate
  89. dl-Thioctic acid
  90. liponate
  91. liponic acid
  92. Rac-lipoic acid
Chemical IUPAC Name 5-(dithiolan-3-yl)pentanoic acid
Chemical Formula C8H14O2S2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Fatty Acids
Sub Class
  • Medium chain fatty acids
Family
  • Mammalian Metabolite
Species
  • disulfide
  • carboxylic acid
  • heterocyclic compound
Biofunction
  • Enzyme co-factor
Application
—
Source
  • Endogenous
Average Molecular Weight 206.326
Monoisotopic Molecular Weight 206.043518
Isomeric SMILES OC(=O)CCCC[C@@H]1CCSS1
Canonical SMILES OC(=O)CCCCC1CCSS1
KEGG Compound ID C00725 Link Image
BioCyc ID LIPOIC-ACID Link Image
BiGG ID 35801 Link Image
Wikipedia Link Lipoic acid Link Image
NuGOwiki Link HMDB01451 Link Image
Metagene Link HMDB01451 Link Image
METLIN ID 126 Link Image
PubChem Compound 864 Link Image
PubChem Substance 11361326 Link Image
ChEBI ID 16494 Link Image
CAS Registry Number 1077-28-7
InChI Identifier InChI=1/C8H14O2S2/c9-8(10)4-2-1-3-7-5-6-11-12-7/h7H,1-6H2,(H,9,10)/t7-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) 60.5 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.127 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 0.224 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 2.75 [Predicted by ALOGPS]; 2.1 [Predicted by PubChem via XLOGP]; 3.40 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1DP2 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • Extracellular
Biofluid Location
  • Blood
Tissue Location
Tissue References
Kidney —
Liver —
Muscle —
Nerve Cells —
Placenta —
Skeletal Muscle —
Concentrations (Normal)
Biofluid Blood
Value 0.077 +/- 0.017 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Ammonia Recycling SMP00009 Link Image map00910 Link Image
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
General References
  1. Henriksen EJ, Saengsirisuwan V: Exercise training and antioxidants: relief from oxidative stress and insulin resistance. Exerc Sport Sci Rev. 2003 Apr;31(2):79-84. [PubMed Link Image]
  2. Arner ES, Nordberg J, Holmgren A: Efficient reduction of lipoamide and lipoic acid by mammalian thioredoxin reductase. Biochem Biophys Res Commun. 1996 Aug 5;225(1):268-74. [PubMed Link Image]
  3. Loginov AS, Nilova TV, Bendikov EA, Petrakov AV: [Pharmacokinetics of preparations of lipoic acid and their effect on ATP synthesis, processes of microsomal and cytosol oxidation in hepatocytes in liver damage in man] Farmakol Toksikol. 1989 Jul-Aug;52(4):78-82. [PubMed Link Image]
  4. Baker H, Deangelis B, Baker ER, Hutner SH: A practical assay of lipoate in biologic fluids and liver in health and disease. Free Radic Biol Med. 1998 Sep;25(4-5):473-9. [PubMed Link Image]
  5. Konrad D: Utilization of the insulin-signaling network in the metabolic actions of alpha-lipoic acid-reduction or oxidation? Antioxid Redox Signal. 2005 Jul-Aug;7(7-8):1032-9. [PubMed Link Image]
  6. Bruggraber SF, Leung PS, Amano K, Quan C, Kurth MJ, Nantz MH, Benson GD, Van de Water J, Luketic V, Roche TE, Ansari AA, Coppel RL, Gershwin ME: Autoreactivity to lipoate and a conjugated form of lipoate in primary biliary cirrhosis. Gastroenterology. 2003 Dec;125(6):1705-13. [PubMed Link Image]
  7. Redden PR, Melanson RL, Douglas JA, Dick AJ: Acyloxymethyl acidic drug derivatives: in vitro hydrolytic reactivity. Int J Pharm. 1999 Apr 15;180(2):151-60. [PubMed Link Image]
  8. Tankova T, Cherninkova S, Koev D: Treatment for diabetic mononeuropathy with alpha-lipoic acid. Int J Clin Pract. 2005 Jun;59(6):645-50. [PubMed Link Image]
  9. Chevion S, Hofmann M, Ziegler R, Chevion M, Nawroth PP: The antioxidant properties of thioctic acid: characterization by cyclic voltammetry. Biochem Mol Biol Int. 1997 Feb;41(2):317-27. [PubMed Link Image]
  10. Barbiroli B, Medori R, Tritschler HJ, Klopstock T, Seibel P, Reichmann H, Iotti S, Lodi R, Zaniol P: Lipoic (thioctic) acid increases brain energy availability and skeletal muscle performance as shown by in vivo 31P-MRS in a patient with mitochondrial cytopathy. J Neurol. 1995 Jul;242(7):472-7. [PubMed Link Image]
  11. Burke DG, Chilibeck PD, Parise G, Tarnopolsky MA, Candow DG: Effect of alpha-lipoic acid combined with creatine monohydrate on human skeletal muscle creatine and phosphagen concentration. Int J Sport Nutr Exerc Metab. 2003 Sep;13(3):294-302. [PubMed Link Image]
  12. Teichert J, Tuemmers T, Achenbach H, Preiss C, Hermann R, Ruus P, Preiss R: Pharmacokinetics of alpha-lipoic acid in subjects with severe kidney damage and end-stage renal disease. J Clin Pharmacol. 2005 Mar;45(3):313-28. [PubMed Link Image]
  13. Haj-Yehia AI, Assaf P, Nassar T, Katzhendler J: Determination of lipoic acid and dihydrolipoic acid in human plasma and urine by high-performance liquid chromatography with fluorimetric detection. J Chromatogr A. 2000 Feb 18;870(1-2):381-8. [PubMed Link Image]
  14. Nagamatsu M, Nickander KK, Schmelzer JD, Raya A, Wittrock DA, Tritschler H, Low PA: Lipoic acid improves nerve blood flow, reduces oxidative stress, and improves distal nerve conduction in experimental diabetic neuropathy. Diabetes Care. 1995 Aug;18(8):1160-7. [PubMed Link Image]
  15. Steinmann B, Gitzelmann R: Strychnine treatment attempted in newborn twins with severe nonketotic hyperglycinemia. Helv Paediatr Acta. 1979;34(6):589-99. [PubMed Link Image]
  16. Lee WJ, Lee IK, Kim HS, Kim YM, Koh EH, Won JC, Han SM, Kim MS, Jo I, Oh GT, Park IS, Youn JH, Park SW, Lee KU, Park JY: Alpha-lipoic acid prevents endothelial dysfunction in obese rats via activation of AMP-activated protein kinase. Arterioscler Thromb Vasc Biol. 2005 Dec;25(12):2488-94. Epub 2005 Oct 13. [PubMed Link Image]
  17. McCormick DB: A trail of research on cofactors: an odyssey with friends. J Nutr. 2000 Feb;130(2S Suppl):323S-330S. [PubMed Link Image]
  18. Semenova TV, Azhitskii GIu, Sarnatskaia VV, Nikolaev VG: [Effect of various specific agents on the heat stability of human serum albumin] Ukr Biokhim Zh. 1993 Sep-Oct;65(5):26-30. [PubMed Link Image]
  19. Wikipedia Link Image
Metabolic Enzymes
  1. Pyruvate dehydrogenase protein X component, mitochondrial precursor
  2. Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor
  3. NADPH--cytochrome P450 reductase
  4. Dihydrolipoyllysine-residue succinyltransferase component of 2- oxoglutarate dehydrogenase complex, mitochondrial precursor
  5. Glycine cleavage system H protein, mitochondrial precursor
  6. Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial precursor
  7. 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
  8. Lipoyltransferase 1, mitochondrial
Enzyme 1 [top]
Enzyme 1 ID 5270
Enzyme 1 Name Pyruvate dehydrogenase protein X component, mitochondrial precursor
Enzyme 1 Synonyms
  1. Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex
  2. Lipoyl-containing pyruvate dehydrogenase complex component X
  3. E3-binding protein
  4. E3BP
  5. proX
Enzyme 1 Gene Name PDHX
Enzyme 1 Protein Sequence >Pyruvate dehydrogenase protein X component, mitochondrial precursor 
MAASWRLGCDPRLLRYLVGFPGRRSVGLVKGALGWSVSRGANWRWFHSTQWLRGDPIKIL
MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSK
NIRLGSLIGLIVEEGEDWKHVEIPKDVGPPPPVSKPSEPRPSPEPQISIPVKKEHIPGTL
RFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKQTGKITESRPTPAPTAT
PTAPSPLQATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTESKSTVPH
AYATADCDLGAVLKVRQDLVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPF
IDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNL
GMFGIDEFTAVINPPQACILAVGRFRPVLKLTEDEEGNAKLQQRQLITVTMSSDSRVVDD
ELATRFLKSFKANLENPIRLA
Enzyme 1 Number of Residues 501
Enzyme 1 Molecular Weight 54123
Enzyme 1 Theoretical pI 9.09
Enzyme 1 GO Classification
Function
  • acyltransferase activity
  • binding
  • catalytic activity
  • protein binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Energy production and conversion
Enzyme 1 Specific Function Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 2316040 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O00330 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ODPX_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1506 bp 
ATGGCGGCCTCCTGGAGGCTGGGCTGTGATCCGCGGCTGCTGCGTTATCTTGTGGGCTTC
CCTGGCTGCCGAAGCGTAGGGCTGGTGAAGGGGGCTCTTGGGTGGTCCGTAAGCCGCGGA
GCTAATTGGAGATGGTTTCACAGCACGCAGTGGCTTCGGGGTGATCCCATTAAGATACTA
ATGCCATCACTGTCTCCTACAATGGAAGAAGGAAACATTGTGAAATGGCTGAAAAAGGAA
GGTGAAGCGGTGAGTGCTGGAGATGCATTATGTGAAATTGAGACTGACAAAGCTGTGGTT
ACCTTAGATGCAAGTGATGATGGAATCTTGGCCAAAATCGTGGTTGAAGAAGGAAGTAAA
AATATACGGCTAGGTTCACTAATTGGTTTGATAGTAGAAGAAGGAGAAGATTGGAAACAT
GTTGAAATTCCCAAAGACGTAGGTCCTCCACCACCAGTTTCAAAACCTTCAGAGCCTCGC
CCCTCACCAGAACCACAGATTTCCATCCCTGTCAAGAAGGAACACATACCCGGGACACTA
CGGTTCCGTTTAAGTCCAGCTGCCCGCAATATTCTGGAAAAACACTCACTGGATGCTAGC
CAGGGCACAGCCACTGGCCCTCGGGGGATATTCACTAAAGAGGATGCTCTCAAACTTGTC
CAGTTGAAACAAACGGGCAAGATTACCGAGTCCAGACCAACTCCAGCCCCCACAGCCACT
CCCACAGCACCTTCGCCCCTACAGGCCACATCTGGACCATCTTATCCCCGGCCTGTGATC
CCACCAGTATCAACTCCCGGACAACCCAATGCAGTGGGCACATTCACTGAAATCCCCGCC
AGCAATATTCGAAGAGTTATTGCCAAGAGATTAACTGAATCTAAAAGTACTGTACCTCAT
GCATATGCTACTGCTGACTGTGACCTTGGAGCTGTTTTAAAAGTTAGGCAAGATCTGGTC
AAAGATGACATTAAAGTATCAGTAAATGATTTTATCATCAAGGCAGCAGCTGTTACCCTT
AAACAAATGCCAGATGTTAATGTAAGCTGGGATGGAGAGGGCCCAAAGCAACTGCCATTT
ATTGACATTTCAGTGGCTGTGGCAACAGATAAAGGCTTACTTACTCCAATCATAAAAGAT
GCTGCTGCTAAAGGTATCCAGGAAATTGCTGACTCTGTAAAGGCTCTATCAAAGAAAGCA
AGAGATGGAAAATTGTTGCCTGAAGAATACCAAGGAGGATCTTTTAGTATTTCCAACTTG
GGGATGTTTGGCATCGACGAATTTACTGCAGTGATTAACCCTCCTCAGGCCTGCATTTTG
GCGGTTGGGAGGTTCCGACCTGTGCTGAAGCTCACTGAGGATGAAGAGGGAAATGCCAAA
CTGCAGCAGCGCCAGCTCATAACAGTCACAATGTCAAGTGACAGTCGAGTGGTTGATGAC
GAACTGGCAACCAGGTTTCTTAAAAGTTTTAAAGCAAACCTAGAGAATCCTATCCGACTT
GCCTAG
Enzyme 1 GenBank Gene ID AF001437 Link Image
Enzyme 1 GeneCard ID PDHX Link Image
Enzyme 1 GenAtlas ID PDHX Link Image
Enzyme 1 HGNC ID HGNC:21350 Link Image
Enzyme 1 Chromosome Location 11
Enzyme 1 Locus 11p13
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Harris RA, Bowker-Kinley MM, Wu P, Jeng J, Popov KM: Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate dehydrogenase complex. DNA-derived amino acid sequence, expression, and reconstitution of the pyruvate dehydrogenase complex. J Biol Chem. 1997 Aug 8;272(32):19746-51. [PubMed Link Image]
  2. Aral B, Benelli C, Ait-Ghezala G, Amessou M, Fouque F, Maunoury C, Creau N, Kamoun P, Marsac C: Mutations in PDX1, the human lipoyl-containing component X of the pyruvate dehydrogenase-complex gene on chromosome 11p1, in congenital lactic acidosis. Am J Hum Genet. 1997 Dec;61(6):1318-26. [PubMed Link Image]
  3. Ling M, McEachern G, Seyda A, MacKay N, Scherer SW, Bratinova S, Beatty B, Giovannucci-Uzielli ML, Robinson BH: Detection of a homozygous four base pair deletion in the protein X gene in a case of pyruvate dehydrogenase complex deficiency. Hum Mol Genet. 1998 Mar;7(3):501-5. [PubMed Link Image]
  4. Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5284
Enzyme 2 Name Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor
Enzyme 2 Synonyms
  1. Pyruvate dehydrogenase complex E2 subunit
  2. PDCE2
  3. E2
  4. Dihydrolipoamide S- acetyltransferase component of pyruvate dehydrogenase complex
  5. PDC- E2
  6. 70 kDa mitochondrial autoantigen of primary biliary cirrhosis
  7. PBC
  8. M2 antigen complex 70 kDa subunit
Enzyme 2 Gene Name DLAT
Enzyme 2 Protein Sequence >Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor 
MSPHCSTTYLRTLGRTTMFWKTTEGRDGKMAVQEFSEFGLLLQLLGSPGRRYYSLPPHQK
VPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEG
TRDVPIGAIICITVGKPEDIEAFKNYTLDSSAAPTPQAAPAPTPAATASPPTPSAQAPGS
SYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLA
KILVPEGTRDVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTP
QPLAPTPSTPCPATPAGPKGRVFVDPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV
PSKVAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVN
MGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSV
AVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGI
KNFSAIINPPQACILAIGASEDKLVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLA
EFRKYLEKPITMLL
Enzyme 2 Number of Residues 614
Enzyme 2 Molecular Weight 65782
Enzyme 2 Theoretical pI 5.95
Enzyme 2 GO Classification
Function
  • S-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • binding
  • catalytic activity
  • dihydrolipoyllysine-residue acetyltransferase activity
  • protein binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
  • protein complex
  • pyruvate dehydrogenase complex
Enzyme 2 General Function Energy production and conversion
Enzyme 2 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)
Enzyme 2 Pathways
Enzyme 2 Reactions
  • acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 35360 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P10515 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ODP2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1848 bp 
CGAGTGACCTCGCGATCTGGCCCGGCTCCCGCTCGTCGCAACAGCGTGACTACAGGGTAT
GGCGGGGTCCGGGCACTGTGCGGCTGGACCCCCAGTTCTGGGGCCACGCCGCGGAACCGC
TTACTGCTGCAGCTTTTGGGGTCGCCCGGCCGCCGCTATTACAGTCTTCCCCCGCATCAG
AAGGTTCCATTGCCTTCTCTTTCCCCCACAATGCAGGCAGGCACCATAGCCCGTTGGAAA
AAAAAAGAGGGGGACAAAATCAATGAAGGTGACCTAATTGCAGAGGTTGAAACTGATAAA
GCCACTGTTGGATTTGAGAGCCTGGAGGAGTGTTATATGGCAAAGATACTTGTTGCTGAA
GGTACCAGGGATGTTCCCATCGGAGCGATCATCTGTATCACAGTTGGCAAGCCTGAGGAT
ATTGAGGCCTTTAAAAATTATACACTGGATTCCTCAGCAGCACCTACCCCACAAGCGGCC
CCAGCACCAACCCCTGCTGCCACTGCTTCGCCACCTACACCTTCTGCTCAGGCTCCTGGT
AGCTCATATCCCCCTCACATGCAGGTACTTCTTCCTGCCCTCTCTCCCACCATGACCATG
GGCACAGTTCAGAGATGGGAAAAAAAAGTGGGTGAGAAGCTAAGTGAAGGAGACTTACTG
GCAGAGATAGAAACTGACAAAGCCACTATAGGTTTTGAAGTACAGGAAGAAGGTTATCTG
GCAAAAATCCTGGTCCCTGAAGGCACAAGAGATGTCCCTCTAGGAACCCCACTCTGTATC
ATTGTAGAAAAAGAGGCAGATATATCAGCATTTGCTGACTATAGGCCAACCGAAGTAACA
GATTTAAAACCACAAGTGCCACCACCTACCCCACCCCCGGTGGCCGCTGTTCCTCCAACT
CCCCAGCCTTTAGCTCCTACACCTTCAGCACCCTGCCCAGCTACTCCTGCTGGACCAAAG
GGAAGGGTGTTTGTTAGCCCTCTTGCAAAGAAGTTGGCAGTAGAGAAAGGGATTGATCTT
ACACAAGTAAAAGGGACAGGACCAGATGGTAGAATCACCAAGAAGGATATCGACTCTTTT
GTGCCTAGTAAAGTTGCTCCTGCTCCGGCAGCTGTTGTGCCTCCCACAGGTCCTGGAATG
GCACCAGTTCCTACAGGTGTCTTCACAGATATCCCAATCAGCAACATTCGTCGGGTTATT
GCACAGCGATTAATGCAATCAAAGCAAACCATACCTCATTATTACCTTTCTATCGATGTA
AATATGGGAGAAGTTTTGTTGGTACGGAAAGAACTTAATAAGATATTAGAAGGGAGAAGC
AAAATTTCTGTCAATGACTTCATCATAAAAGCTTCAGCTTTGGCATGTTTAAAAGTTCCC
GAAGCAAATTCTTCTTGGATGGACACAGTTATAAGACAAAATCATGTTGTTGATGTCAGT
GTTGCGGTCAGTACTCCTGCAGGACTCATCACACCTATTGTGTTTAATGCACATATAAAA
GGAGTGGAAACCATTGCTAATGATGTTGTTTCTTTAGCAACCAAAGCAAGAGAGGGTAAA
CTACAGCCACATGAATTCCAGGGTGGCACTTTTACGATCTCCAATTTAGGAATGTTTGGA
ATTAAGAATTTCTCTGCTATTATTAACCCACCTCAAGCATGTATTTTGGCAATTGGTGCT
TCAGAGGATAAACTGGTCCCTGCAGATAATGAAAAAGGGTTTGATGTGGCTAGCATGATG
TCTGTTACACTCAGTTGTGATCACCGGGTGGTGGATGGAGCAGTTGGAGCCCAGTGGCTT
GCTGAGTTTAGAAAGTACCTTGAAAAACCTATCACTATGTTGTTGTAA
Enzyme 2 GenBank Gene ID Y00978 Link Image
Enzyme 2 GeneCard ID DLAT Link Image
Enzyme 2 GenAtlas ID DLAT Link Image
Enzyme 2 HGNC ID HGNC:2896 Link Image
Enzyme 2 Chromosome Location 11
Enzyme 2 Locus 11q23.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Coppel RL, McNeilage LJ, Surh CD, Van de Water J, Spithill TW, Whittingham S, Gershwin ME: Primary structure of the human M2 mitochondrial autoantigen of primary biliary cirrhosis: dihydrolipoamide acetyltransferase. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7317-21. [PubMed Link Image]
  2. Thekkumkara TJ, Ho L, Wexler ID, Pons G, Liu TC, Patel MS: Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex. FEBS Lett. 1988 Nov 21;240(1-2):45-8. [PubMed Link Image]
  3. Howard MJ, Fuller C, Broadhurst RW, Perham RN, Tang JG, Quinn J, Diamond AG, Yeaman SJ: Three-dimensional structure of the major autoantigen in primary biliary cirrhosis. Gastroenterology. 1998 Jul;115(1):139-46. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5415
Enzyme 3 Name NADPH--cytochrome P450 reductase
Enzyme 3 Synonyms
  1. CPR
  2. P450R
Enzyme 3 Gene Name POR
Enzyme 3 Protein Sequence >NADPH--cytochrome P450 reductase 
MGDSHVDTSSTVSEAVAEEVSLFSMTDMILFSLIVGLLTYWFLFRKKKEEVPEFTKIQTL
TSSVRESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLA
DLSSLPEIDNALVVFCMATYGEGDPTDNAQDFYDWLQETDVDLSGVKFAVFGLGNKTYEH
FNAMGKYVDKRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEHFGVEATGEES
SIRQYELVVHTDIDAAKVYMGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHL
MHLELDISDSKIRYESGDHVAVYPANDSALVNQLGKILGADLDVVMSLNNLDEESNKKHP
FPCPTSYRTALTYYLDITNPPRTNVLYELAQYASEPSEQELLRKMASSSGEGKELYLSWV
VEARRHILAILQDCPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVVVEYET
KAGRINKGVATNWLRAKEPAGENGGRALVPMFVRKSQFRLPFKATTPVIMVGPGTGVAPF
IGFIQERAWLRQQGKEVGETLLYYGCRRSDEDYLYREELAQFHRDGALTQLNVAFSREQS
HKVYVQHLLKQDREHLWKLIEGGAHIYVCGDARNMARDVQNTFYDIVAELGAMEHAQAVD
YIKKLMTKGRYSLDVWS
Enzyme 3 Number of Residues 677
Enzyme 3 Molecular Weight 76691
Enzyme 3 Theoretical pI 5.28
Enzyme 3 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • electron transporter activity
  • nucleotide binding
  • oxidoreductase activity
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Inorganic ion transport and metabolism
Enzyme 3 Specific Function This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-39
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 247307 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P16435 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name NCPR_HUMAN Link Image
Enzyme 3 PDB ID 1AMO Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2031 bp 
GGAGACTCCCACGTGGACACCAGCTCCACCGTGTCCGAGGCGGTGGCCGAAGAAGTATCT
CTTTTCAGCATGACGGACATGATTCTGTTTTCGCTCATCGTGGGTCTCCTAACCTACTGG
TTCCTCTTCAGAAAGAAAAAAGAAGAAGTCCCCGAGTTCACCAAAATTCAGACATTGACC
TCCTCTGTCAGAGAGAGCAGCTTTGTGGAAAAGATGAAGAAAACGGGGAGGAACATCATC
GTGTTCTACGGCTCCCAGACGGGGACTGCAGAGGAGTTTGCCAACCGCCTGTCCAAGGAC
GCCCACCGCTACGGGATGCGAGGCATGTCAGCGGACCCTGAGGAGTATGACCTGGCCGAC
CTGAGCAGCCTGCCAGAGATCGACAACGCCCTGGTGGTTTTCTGCATGGCCACCTACGGT
GAGGGAGACCCCACCGACAATGCCCAGGACTTCTACGACTGGCTGCAGGAGACAGACGTG
GATCTCTCTGGGGTCAAGTTCGCGGTGTTTGGTCTTGGGAACAAGACCTACGAGCACTTC
AATGCCATGGGCAAGTACGTGGACAAGCGGCTGGAGCAGCTCGGCGCCCAGCGCATCTTT
GAGCTGGGGTTGGGCGACGACGATGGGAACTTGGAGGAGGACTTCATCACCTGGCGAGAG
CAGTTCTGGCCGGCCGTGTGTGAACACTTTGGGGTGGAAGCCACTGGCGAGGAGTCCAGC
ATTCGCCAGTACGAGCTTGTGGTCCACACCGACATAGATGCGGCCAAGGTGTACATGGGG
GAGATGGGCCGGCTGAAGAGCTACGAGAACCAGAAGCCCCCCTTTGATGCCAAGAATCCG
TTCCTGGCTGCAGTCACCACCAACCGGAAGCTGAACCAGGGAACCGAGCGCCACCTCATG
CACCTGGAATTGGACATCTCGGACTCCAAAATCAGGTATGAATCTGGGGACCACGTGGCT
GTGTACCCAGCCAACGACTCTGCTCTCGTCAACCAGCTGGGCAAAATCCTGGGTGCCGAC
CTGGACGTCGTCATGTCCCTGAACAACCTGGATGAGGAGTCCAACAAGAAGCACCCATTC
CCGTGCCCTACGTCCTACCGCACGGCCCTCACCTACTACCTGGACATCACCAACCCGCCG
CGTACCAACGTGCTGTACGAGCTGGCGCAGTACGCCTCGGAGCCCTCGGAGCAGGAGCTG
CTGCGCAAGATGGCCTCCTCCTCCGGCGAGGGCAAGGAGCTGTACCTGAGCTGGGTGGTG
GAGGCCCGGAGGCACATCCTGGCCATCCTGCAGGACTGCCCGTCCCTGCGGCCCCCCATC
GACCACCTGTGTGAGCTGCTGCCGCGCCTGCAGGCCCGCTACTACTCCATCGCCTCATCC
TCCAAGGTCCACCCCAACTCTGTGCACATCTGTGCGGTGGTTGTGGAGTACGAGACCAAG
GCCGGCCGCATCAACAAGGGCGTGGCCACCAACTGGCTGCGGGCCAAGGAGCCTGTCGGG
GAGAACGGCGGCCGTGCGCTGGTGCCCATGTTCGTGCGCAAGTCCCAGTTACGCCTGCCC
TTCAAGGCCACCACGCCTGTCATCATGGTGGGCCCCGGCACCGGGTGGCACCCTTTCATA
GGCTTCATCCAGGAGCGGGCCTGGCTGCGACAGCAGGGCAAGGAGGTGGGGGAGACGCTG
CTGTACTACGGCTGCCGCCGCTCGGATGAGGACTACCTGTACCGGGAGGAGCTGGCGCAG
TTCCACAGGGACGGTGCGCTCACCCAGCTCAACGTGGCCTTCTCCCGGGAGCAGTCCCAC
AAGGTCTACGTCCAGCACCTGCTAAAGCAAGACCGAGAGCACCTGTGGAAGTTGATCGAA
GGCGGTGCCCACATCTACGTCTGTGGGGATGCACGGAACATGGCCAGGGATGTGCAGAAC
ACCTTCTACGACATCGTGGCTGAGCTCGGGGCCATGGAGCACGCGCAGGCGGTGGACTAC
ATCAAGAAACTGATGACCAAGGGCCGCTACTCCCTGGACGTGTGGAGCTAG
Enzyme 3 GenBank Gene ID S90469 Link Image
Enzyme 3 GeneCard ID POR Link Image
Enzyme 3 GenAtlas ID POR Link Image
Enzyme 3 HGNC ID HGNC:9208 Link Image
Enzyme 3 Chromosome Location 7
Enzyme 3 Locus 7q11.2
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Shephard EA, Palmer CN, Segall HJ, Phillips IR: Quantification of cytochrome P450 reductase gene expression in human tissues. Arch Biochem Biophys. 1992 Apr;294(1):168-72. [PubMed Link Image]
  2. Haniu M, McManus ME, Birkett DJ, Lee TD, Shively JE: Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: complete sequence of human enzyme and NADPH-binding sites. Biochemistry. 1989 Oct 17;28(21):8639-45. [PubMed Link Image]
  3. Zhao Q, Modi S, Smith G, Paine M, McDonagh PD, Wolf CR, Tew D, Lian LY, Roberts GC, Driessen HP: Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution. Protein Sci. 1999 Feb;8(2):298-306. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6227
Enzyme 4 Name Dihydrolipoyllysine-residue succinyltransferase component of 2- oxoglutarate dehydrogenase complex, mitochondrial precursor
Enzyme 4 Synonyms
  1. Dihydrolipoamide succinyltransferase component of 2- oxoglutarate dehydrogenase complex
  2. E2
  3. E2K
Enzyme 4 Gene Name DLST
Enzyme 4 Protein Sequence >Dihydrolipoyllysine-residue succinyltransferase component of 2- oxoglutarate dehydrogenase complex, mitochondrial precursor 
MLSRSRCVSRAFSAPLSAFQKGNCPLGRRSLPGVSLCQGPGYPNSRKVVINNSVFSVRFF
RTTAVCKDDLVTVKTPAFAESVTEGDVRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAN
GVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAAVPPPAAPI
PTQMPPVPSPSQPPSGKPVSAVKPTVAPPLADAGAGKGLRSEHREKMNRMRQRIAQRLKE
AQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKASAFALQEQPVVNA
VIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELA
IEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVAL
TYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL
Enzyme 4 Number of Residues 453
Enzyme 4 Molecular Weight 48641
Enzyme 4 Theoretical pI 9.20
Enzyme 4 GO Classification
Function
  • S-acyltransferase activity
  • S-succinyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • dihydrolipoyllysine-residue succinyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • cellular metabolism
  • energy derivation by oxidation of organic compounds
  • generation of precursor metabolites and energy
  • main pathways of carbohydrate metabolism
  • metabolism
  • physiological process
  • tricarboxylic acid cycle
Component
  • oxoglutarate dehydrogenase complex
  • protein complex
Enzyme 4 General Function Energy production and conversion
Enzyme 4 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 3 enzymatic components:2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3)
Enzyme 4 Pathways
Enzyme 4 Reactions
  • succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 499719 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P36957 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name ODO2_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1362 bp 
ATGCTGTCCCGATCCCGCTGTGTGTCTCGGGCGTTCAGCGCTCCGCTCTCCGCCTTCCAG
AAGGGGAACTGCCCTCTAGGGAGACGTTCCCTGCCTGGGGTCTCCTTATGCCAGGGACCA
GGTTACCCTAACAGCAGGAAGGTTGTCATTAACAACAGTGTCTTCAGTGTTCGCTTTTTC
AGAACTACAGCTGTATGCAAGGATGACTTGGTTACAGTCAAAACCCCAGCGTTTGCAGAA
TCTGTCACAGAGGGAGATGTCAGGTGGGAGAAAGCTGTTGGAGACACAGTTGCAGAAGAT
GAAGTGGTTTGTGAGATTGAAACTGACAAGACATCTGTGCAGGTTCCATCACCAGCAAAT
GGCGTGATTGAAGCTCTTTTGGTACCTGATGGGACAAAAGTCGAAGGAGGCACTCCACTT
TTCACACTCAGGAAAACTGGTGCTGCTCCTGCTAAGGCCAAGCCGGCTGAAGCTCCTGCT
GCTGCAGCCCCAAAAGCAGAACCTACAGCAGCGGCAGTTCCTCCCCCTGCAGCACCCATA
CCCACTCAGATGCCACCGGTGCCCTCGCCCTCACAGCCTCCTTCTGGCAAACCTGTGTCT
GCAGTAAAACCCACTGTTGCCCCACCACTAGCTGACGCAGGAGCTGGCAAAGGTCTGCGT
TCAGAACATCGGGAGAAAATGAACAGGATGCGGCAACGCATTGCTCAGCGTCTGAAGGAG
GCCCAGAATACATGTGCAATGCTGACAACTTTTAATGAGATTGACATGAGTAACATCCAG
GAGATGAGGGCTCGGCACAAAGAGGCTTTTTTGAAGAAACATAACCTCAAACTAGGCTTC
ATGTCGGCATTTGTGAAGGCCTCAGCCTTTGCCTTGCAGGAACAGCCTGTTGTAAATGCA
GTGATTGACGACACAACCAAAGAGGTGGTGTATAGGGATTATATTGACATCAGTGTTGCA
GTGGCCACCCCAAGGGGTCTGGTGGTTCCAGTCATCAGGAATGTGGAAGCTATGAATTTT
GCAGATATTGAACGGACCATCACTGAACTGGGAGAGAAGGCCCGAAAGAATGAACTTGCC
ATTGAAGATATGGATGGCGGTACCTTCACCATTAGCAATGGAGGCGTTTTTGGCTCGCTC
TTTGGAACAACCATTATCAACCCCCCTCAGTCTGCCATCCTGGGGATGCATGGCATCTTT
GACAGGCCAGTGGCTATAGGAGGCAAGGTAGAGGTGCGGCCCATGATGTACGTGGCACTG
ACCTATGATCACCGGCTGATTGATGGCAGAGAGGCTGTGACTTTCCTCCGCAAAATCAAG
GCAGCGGTAGAGGATCCCAGAGTCCTCCTCCTGGATCTTTAG
Enzyme 4 GenBank Gene ID D16373 Link Image
Enzyme 4 GeneCard ID DLST Link Image
Enzyme 4 GenAtlas ID DLST Link Image
Enzyme 4 HGNC ID HGNC:2911 Link Image
Enzyme 4 Chromosome Location 14
Enzyme 4 Locus 14q24.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Nakano K, Matuda S, Sakamoto T, Takase C, Nakagawa S, Ohta S, Ariyama T, Inazawa J, Abe T, Miyata T: Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3. Biochim Biophys Acta. 1993 Dec 14;1216(3):360-8. [PubMed Link Image]
  2. Nakano K, Takase C, Sakamoto T, Nakagawa S, Inazawa J, Ohta S, Matuda S: Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex. Eur J Biochem. 1994 Aug 15;224(1):179-89. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 8590
Enzyme 5 Name Glycine cleavage system H protein, mitochondrial precursor
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name GCSH
Enzyme 5 Protein Sequence >Glycine cleavage system H protein, mitochondrial precursor 
MALRVVRSVRALLCTLRAVPLPAAPCPPRPWQLGVGAVRTLRTGPALLSVRKFTEKHEWV
TTENGIGTVGISNFAQEALGDVVYCSLPEVGTKLNKQDEFGALESVKAASELYSPLSGEV
TEINEALAENPGLVNKSCYEDGWLIKMTLSNPSELDELMSEEAYEKYIKSIEE
Enzyme 5 Number of Residues 173
Enzyme 5 Molecular Weight 18911
Enzyme 5 Theoretical pI 4.56
Enzyme 5 GO Classification
Function
—
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • glycine catabolism
  • glycine metabolism
  • metabolism
  • physiological process
  • serine family amino acid metabolism
Component
  • glycine cleavage complex
  • protein complex
Enzyme 5 General Function Amino acid transport and metabolism
Enzyme 5 Specific Function The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-18
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 184348 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P23434 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name GCSH_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >522 bp 
ATGGCGCTGCGAGTGGTGCGGAGCGTGCGGGCCCTGCTCTGCACCCTGCGCGCGGTCCCG
TTACCCGCCGCGCCCTGCCCGCCGAGGCCCTGGCAGCTGGGGGTGGGCGCCGTCCGTACG
CTGCGCACTGGACCCGCTCTGCTCTCGGTGCGTAAATTCACAGAGAAACACGAATGGGTA
ACAACAGAAAATGGCATTGGAACAGTGGGAATCAGCAATTTTGCACAGGAAGCGTTGGGA
GATGTTGTTTATTGTAGTCTCCCTGAAGTTGGGACAAAATTGAACAAACAAGATGAGTTT
GGTGCTTTGGAAAGTGTGAAAGCTGCTAGTGAACTCTATTCTCCTTTATCAGGAGAAGTA
ACTGAAATTAATGAAGCTCTTGCAGAAAATCCAGGACTTGTAAACAAATCTTGTTATGAA
GATGGTTGGCTGATCAAGATGACACTGAGTAACCCTTCAGAACTAGATGAACTTATGAGT
GAAGAAGCATATGAGAAATACATAAAATCTATTGAGGAGTGA
Enzyme 5 GenBank Gene ID M69175 Link Image
Enzyme 5 GeneCard ID GCSH Link Image
Enzyme 5 GenAtlas ID GCSH Link Image
Enzyme 5 HGNC ID HGNC:4208 Link Image
Enzyme 5 Chromosome Location 16
Enzyme 5 Locus 16q23.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Koyata H, Hiraga K: The glycine cleavage system: structure of a cDNA encoding human H-protein, and partial characterization of its gene in patients with hyperglycinemias. Am J Hum Genet. 1991 Feb;48(2):351-61. [PubMed Link Image]
  2. Fujiwara K, Okamura-Ikeda K, Hayasaka K, Motokawa Y: The primary structure of human H-protein of the glycine cleavage system deduced by cDNA cloning. Biochem Biophys Res Commun. 1991 Apr 30;176(2):711-6. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 8614
Enzyme 6 Name Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial precursor
Enzyme 6 Synonyms
  1. Dihydrolipoyllysine-residue
  2. 2-methylpropanoyltransferase
  3. E2
  4. Dihydrolipoamide branched chain transacylase
  5. BCKAD E2 subunit
Enzyme 6 Gene Name DBT
Enzyme 6 Protein Sequence >Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial precursor 
MAAVRMLRTWSRNAGKLICVRYFQTCGNVHVLKPNYVCFFGYPSFKYSHPHHFLKTTAAL
RGQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKK
LYYNLDDIAYVGKPLVDIETEALKDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRL
AMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKVEIMPPPPKPKDMTVPIL
VSKPPVFTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEIDLTELVKLREELKPIAFA
RGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVK
NVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTFAKPVIMPPEVAI
GALGSIKAIPRFNQKGEVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLD
LK
Enzyme 6 Number of Residues 482
Enzyme 6 Molecular Weight 53488
Enzyme 6 Theoretical pI 8.75
Enzyme 6 GO Classification
Function
  • acyltransferase activity
  • binding
  • catalytic activity
  • protein binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 6 General Function Energy production and conversion
Enzyme 6 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)
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • 2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-15
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID P11182 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name ODB2_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID X66785 Link Image
Enzyme 6 GeneCard ID DBT Link Image
Enzyme 6 GenAtlas ID DBT Link Image
Enzyme 6 HGNC ID HGNC:2698 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 1p31
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Lau KS, Chuang JL, Herring WJ, Danner DJ, Cox RP, Chuang DT: The complete cDNA sequence for dihydrolipoyl transacylase (E2) of human branched-chain alpha-keto acid dehydrogenase complex. Biochim Biophys Acta. 1992 Oct 20;1132(3):319-21. [PubMed Link Image]
  2. Hummel KB, Litwer S, Bradford AP, Aitken A, Danner DJ, Yeaman SJ: Nucleotide sequence of a cDNA for branched chain acyltransferase with analysis of the deduced protein structure. J Biol Chem. 1988 May 5;263(13):6165-8. [PubMed Link Image]
  3. Danner DJ, Litwer S, Herring WJ, Pruckler J: Construction and nucleotide sequence of a cDNA encoding the full-length preprotein for human branched chain acyltransferase. J Biol Chem. 1989 May 5;264(13):7742-6. [PubMed Link Image]
  4. Nobukuni Y, Mitsubuchi H, Endo F, Matsuda I: Complete primary structure of the transacylase (E2b) subunit of the human branched chain alpha-keto acid dehydrogenase complex. Biochem Biophys Res Commun. 1989 Jun 30;161(3):1035-41. [PubMed Link Image]
  5. Lau KS, Griffin TA, Hu CW, Chuang DT: Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain alpha-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs. Biochemistry. 1988 Mar 22;27(6):1972-81. [PubMed Link Image]
  6. Lau KS, Herring WJ, Chuang JL, McKean M, Danner DJ, Cox RP, Chuang DT: Structure of the gene encoding dihydrolipoyl transacylase (E2) component of human branched chain alpha-keto acid dehydrogenase complex and characterization of an E2 pseudogene. J Biol Chem. 1992 Nov 25;267(33):24090-6. [PubMed Link Image]
  7. Wynn RM, Kochi H, Cox RP, Chuang DT: Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence. Biochim Biophys Acta. 1994 Sep 28;1201(1):125-8. [PubMed Link Image]
  8. Chang CF, Chou HT, Chuang JL, Chuang DT, Huang TH: Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex. J Biol Chem. 2002 May 3;277(18):15865-73. Epub 2002 Feb 11. [PubMed Link Image]
  9. Fisher CW, Lau KS, Fisher CR, Wynn RM, Cox RP, Chuang DT: A 17-bp insertion and a Phe215----Cys missense mutation in the dihydrolipoyl transacylase (E2) mRNA from a thiamine-responsive maple syrup urine disease patient WG-34. Biochem Biophys Res Commun. 1991 Jan 31;174(2):804-9. [PubMed Link Image]
  10. Tsuruta M, Mitsubuchi H, Mardy S, Miura Y, Hayashida Y, Kinugasa A, Ishitsu T, Matsuda I, Indo Y: Molecular basis of intermittent maple syrup urine disease: novel mutations in the E2 gene of the branched-chain alpha-keto acid dehydrogenase complex. J Hum Genet. 1998;43(2):91-100. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 14991
Enzyme 7 Name 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
Enzyme 7 Synonyms
  1. Beta-ketoacyl-ACP synthase
Enzyme 7 Gene Name OXSM
Enzyme 7 Protein Sequence >3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial 
MSNCLQNFLKITSTRLLCSRLCQQLRSKRKFFGTVPISRLHRRVVITGIGLVTPLGVGTH
LVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRGSDEGQFNEQNFVSKSDIKSMSSPTI
MAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFV
PKILVNMAAGQVSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCI
SPLSLAGFSRARALSTNSDPKLACRPFHPKRDGFVMGEGAAVLVLEEYEHAVQRRARIYA
EVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN
KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEF
DLNYVPLKAQEWKTEKRFIGLTNSFGFGGTNATLCIAGL
Enzyme 7 Number of Residues 459
Enzyme 7 Molecular Weight 48843
Enzyme 7 Theoretical pI 7.72
Enzyme 7 GO Classification
Function
  • catalytic activity
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid biosynthesis
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
—
Enzyme 7 General Function Lipid transport and metabolism
Enzyme 7 Specific Function May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 7020821 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9NWU1 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name OXSM_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1380 bp 
ATGTCCAACTGCCTGCAAAATTTCCTGAAAATTACAAGCACTCGTCTTCTATGTTCAAGA
TTATGCCAACAGTTAAGAAGTAAAAGGAAGTTTTTCGGAACTGTGCCAATATCCAGATTG
CATAGGCGAGTTGTCATTACAGGCATTGGCTTAGTGACTCCTCTTGGTGTTGGAACTCAC
CTGGTTTGGGATCGTCTTATCGGAGGAGAGAGTGGAATTGTTTCACTGGTTGGTGAAGAG
TATAAGAGTATCCCTTGCAGTGTTGCTGCTTATGTGCCAAGAGGTAGTGATGAAGGTCAG
TTCAATGAACAAAACTTTGTGTCCAAATCAGATATCAAGTCCATGTCTTCTCCCACCATC
ATGGCCATTGGGGCTGCAGAATTAGCCATGAAGGATTCTGGCTGGCATCCTCAGTCAGAA
GCTGATCAAGTGGCTACTGGTGTTGCAATTGGCATGGGAATGATTCCTCTTGAAGTTGTT
TCTGAAACTGCTTTGAATTTTCAGACAAAAGGTTACAATAAAGTTAGCCCATTTTTTGTC
CCTAAGATTCTGGTCAATATGGCAGCAGGCCAGGTCAGCATTCGATATAAACTCAAGGGC
CCAAATCATGCAGTATCCACAGCCTGTACCACAGGAGCTCATGCTGTGGGAGACTCATTT
AGATTTATAGCCCATGGTGATGCTGATGTGATGGTGGCTGGAGGTACAGATTCTTGTATT
AGCCCTTTATCTCTTGCTGGGTTTTCCAGAGCCCGGGCTCTGAGCACAAACTCAGATCCC
AAGTTGGCATGTCGACCATTTCATCCAAAGAGAGATGGTTTTGTAATGGGAGAAGGTGCA
GCTGTGCTGGTGCTGGAAGAATATGAACATGCTGTTCAAAGAAGAGCCCGGATCTATGCA
GAAGTTTTGGGCTATGGACTCTCAGGTGATGCTGGTCACATAACTGCCCCTGATCCTGAA
GGAGAAGGTGCCTTAAGGTGTATGGCTGCTGCTTTAAAAGATGCAGGTGTGCAGCCTGAG
GAGATATCCTATATCAATGCACATGCTACTTCCACACCATTGGGAGATGCTGCTGAAAAC
AAAGCTATCAAACATCTCTTCAAAGACCATGCATATGCCCTTGCAGTTTCCTCAACTAAG
GGAGCAACAGGACATCTGCTGGGAGCTGCAGGGGCAGTCGAGGCAGCTTTTACCACATTA
GCTTGTTATTATCAAAAACTACCACCTACTTTAAACCTGGATTGTTCGGAACCAGAATTT
GATCTCAACTATGTTCCACTAAAGGCACAGGAATGGAAAACTGAGAAAAGATTTATTGGC
CTCACCAATTCCTTTGGTTTTGGTGGTACTAATGCAACACTTTGTATTGCTGGACTGTAG
Enzyme 7 GenBank Gene ID AK000611 Link Image
Enzyme 7 GeneCard ID Q9NWU1 Link Image
Enzyme 7 GenAtlas ID OXSM Link Image
Enzyme 7 HGNC ID HGNC:26063 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 16938
Enzyme 8 Name Lipoyltransferase 1, mitochondrial
Enzyme 8 Synonyms
  1. Lipoate-protein ligase
  2. Lipoate biosynthesis protein
  3. Lipoyl ligase
Enzyme 8 Gene Name LIPT1
Enzyme 8 Protein Sequence >Lipoyltransferase 1, mitochondrial 
MLIPFSMKNCFQLLCNCQVPAAGFKKTVKNGLILQSISNDVYQNLAVEDWIHDHMNLEGK
PILFFWQNSPSVVIGRHQNPWQECNLNLMREEGIKLARRRSGGGTVYHDMGNINLTFFTT
KKKYDRMENLKLIVRALNAVQPQLDVQATKRFDLLLDGQFKISGTASKIGRTTAYHHCTL
LCSTDGTFLSSLLKSPYQGIRSNATASIPSLVKNLLEKDPTLTCEVLMNAVATEYAAYHQ
IDNHIHLINPTDETLFPGINSKAKELQTWEWIYGKTPKFSINTSFHVLYEQSHLEIKVFI
DIKNGRIEICNIEAPDHWLPLEIRDKLNSSLIGSKFCPTETTMLTNILLRTCPQDHKLNS
KWNILCEKIKGIM
Enzyme 8 Number of Residues 373
Enzyme 8 Molecular Weight 42480
Enzyme 8 Theoretical pI 8.48
Enzyme 8 GO Classification
Function
  • catalytic activity
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein modification
Component
—
Enzyme 8 General Function Carbohydrate transport and metabolism
Enzyme 8 Specific Function Catalyzes the transfer of the lipoyl group from lipoyl- AMP to the specific lysine residue of lipoyl domains of lipoate- dependent enzymes
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID Q9Y234 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name LIPT_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AB017566 Link Image
Enzyme 8 GeneCard ID Q9Y234 Link Image
Enzyme 8 GenAtlas ID LIPT1 Link Image
Enzyme 8 HGNC ID HGNC:29569 Link Image
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y: Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene. Eur J Biochem. 1999 Mar;260(3):761-7. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available