You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Record Information
Version3.6
Creation Date2005-11-16 15:48:42 UTC
Update Date2014-10-09 18:45:29 UTC
HMDB IDHMDB00044
Secondary Accession Numbers
  • HMDB14273
  • HMDB29945
Metabolite Identification
Common NameAscorbic acid
DescriptionAscorbic acid is found naturally in citrus fruits and many vegetables and is an essential nutrient in human diets. It is necessary to maintain connective tissue and bone. The biologically active form of ascorbic acid is vitamin C. Vitamin C is a water soluble vitamin. Primates (including humans) and a few other species in all divisions of the animal kingdom, notably the guinea pig, have lost the ability to synthesize ascorbic acid and must obtain it in their food. Vitamin C functions as a reducing agent and coenzyme in several metabolic pathways. Vitamin C is considered an antioxidant. [PubChem] Ascorbic acid is an electron donor for enzymes involved in collagen hydroxylation, biosynthesis of carnitine and norepinephrine, tyrosine metabolism, and amidation of peptide hormones. Ascrobic acid (vitamin C) deficiency causes scurvy. The amount of vitamin C necessary to prevent scurvy may not be adequate to maintain optimal health. The ability of vitamin C to donate electrons also makes it a potent water-soluble antioxidant that readily scavenges free radicals such as molecular oxygen, superoxide, hydroxyl radical, and hypochlorous acid. In this setting, several mechanisms could account for a link between vitamin C and heart disease. One is the relation between LDL oxidation and vitamins C and E. Vitamin C in vitro can recycle vitamin E, which can donate electrons to prevent LDL oxidation in vitro. As the lipid-phase vitamin E is oxidized, it can be regenerated by aqueous vitamin C. Other possibilities are that vitamin C could decrease cholesterol by mechanisms not well characterized, or could improve vasodilatation and vascular reactivity, perhaps by decreasing the interactions of nitric oxide with oxidants. (PMID: 10799361 ).
Structure
Thumb
Synonyms
  1. (+)-ascorbate
  2. (+)-ascorbic acid
  3. (+)-Sodium L-ascorbate
  4. 3-Keto-L-gulofuranolactone
  5. 3-Oxo-L-gulofuranolactone
  6. Adenex
  7. Allercorb
  8. Antiscorbic vitamin
  9. Antiscorbutic vitamin
  10. Arco-cee
  11. Ascoltin
  12. Ascor-B.I.D.
  13. Ascorb
  14. Ascorbajen
  15. Ascorbate
  16. Ascorbic acid
  17. Ascorbicab
  18. Ascorbicap
  19. Ascorbicin
  20. Ascorbin
  21. Ascorbutina
  22. Ascorin
  23. Ascorteal
  24. Ascorvit
  25. C-Level
  26. C-Long
  27. C-Quin
  28. C-Span
  29. C-Vimin
  30. Cantan
  31. Cantaxin
  32. Catavin C
  33. Ce lent
  34. Ce-mi-lin
  35. Ce-vi-sol
  36. Cebicure
  37. Cebid
  38. Cebion
  39. Cebione
  40. Cecon
  41. Cee-caps TD
  42. Cee-vite
  43. Cegiolan
  44. Ceglion
  45. Ceklin
  46. Celaskon
  47. Celin
  48. Cell C
  49. Cemagyl
  50. Cemill
  51. Cenetone
  52. Cenolate
  53. Cereon
  54. Cergona
  55. Cescorbat
  56. Cetamid
  57. Cetane
  58. Cetane-caps TC
  59. Cetane-caps TD
  60. Cetebe
  61. Cetemican
  62. Cevalin
  63. Cevatine
  64. Cevex
  65. Cevi-bid
  66. Cevimin
  67. Cevital
  68. Cevitamate
  69. Cevitamic acid
  70. Cevitamin
  71. Cevitan
  72. Cevitex
  73. Cewin
  74. Chewcee
  75. Ciamin
  76. Cipca
  77. Citriscorb
  78. Citrovit
  79. Colascor
  80. Concemin
  81. Davitamon C
  82. Dora-C-500
  83. Duoscorb
  84. Ferrous ascorbate
  85. gamma-Lactone L-threo-Hex-2-enonate
  86. gamma-Lactone L-threo-Hex-2-enonic acid
  87. HiCee
  88. Hybrin
  89. Ido-C
  90. Juvamine
  91. Kangbingfeng
  92. Kyselina askorbova
  93. L(+)-Ascorbate
  94. L(+)-Ascorbic acid
  95. L-(+)-Ascorbate
  96. L-(+)-Ascorbic acid
  97. L-3-Ketothreohexuronic acid lactone
  98. L-Ascorbate
  99. L-Ascorbic acid
  100. L-Lyxoascorbate
  101. L-Lyxoascorbic acid
  102. L-Threo-ascorbic acid
  103. L-Xyloascorbate
  104. L-Xyloascorbic acid
  105. Laroscorbine
  106. Lemascorb
  107. Liqui-cee
  108. Meri-c
  109. Natrascorb
  110. Natrascorb injectable
  111. Planavit C
  112. Proscorbin
  113. Redoxon
  114. Ribena
  115. Ronotec 100
  116. Rontex 100
  117. Roscorbic
  118. Rovimix C
  119. Scorbacid
  120. Scorbu C
  121. Scorbu-C
  122. Secorbate
  123. Sodascorbate
  124. Suncoat VC 40
  125. Testascorbic
  126. VASC
  127. Vicelat
  128. Vicin
  129. Vicomin C
  130. Viforcit
  131. Viscorin
  132. Viscorin 100M
  133. Vitace
  134. Vitacee
  135. Vitacimin
  136. Vitacin
  137. Vitamin C
  138. Vitamisin
  139. Vitascorbol
  140. Xitix
Chemical FormulaC6H8O6
Average Molecular Weight176.1241
Monoisotopic Molecular Weight176.032087988
IUPAC Name(5R)-5-[(1S)-1,2-dihydroxyethyl]-3,4-dihydroxy-2,5-dihydrofuran-2-one
Traditional Namevitamin C
CAS Registry Number50-81-7
SMILES
[H][C@@]1(OC(=O)C(O)=C1O)[C@@H](O)CO
InChI Identifier
InChI=1S/C6H8O6/c7-1-2(8)5-3(9)4(10)6(11)12-5/h2,5,7-10H,1H2/t2-,5+/m0/s1
InChI KeyCIWBSHSKHKDKBQ-JLAZNSOCSA-N
Chemical Taxonomy
KingdomOrganic Compounds
Super ClassAliphatic Heteromonocyclic Compounds
ClassDihydrofurans
Sub ClassFuranones
Other Descriptors
  • Aliphatic Heteromonocyclic Compounds
Substituents
  • 1,2 Diol
  • Ketone
  • Primary Alcohol
  • Secondary Alcohol
Direct ParentButenolides
Ontology
StatusDetected and Quantified
Origin
  • Drug
  • Food
Biofunction
  • Anti-oxidant
  • Component of Tyrosine metabolism
  • Enzyme co-factor
  • Essential vitamins
  • Free Radical Scavengers
  • Nutrient
  • Vitamins
  • Vitamins (Vitamin C)
Application
  • Dye / Coloring Agent
  • Pharmaceutical
Cellular locations
  • Cytoplasm
  • Extracellular
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point191 °CPhysProp
Boiling PointNot AvailableNot Available
Water Solubility400 mg/mL at 40 °CMERCK INDEX (1996)
LogP-1.85AVDEEF,A (1997)
Predicted Properties
PropertyValueSource
Water Solubility245 g/LALOGPS
logP-1.6ALOGPS
logP-1.9ChemAxon
logS0.14ALOGPS
pKa (Strongest Acidic)4.36ChemAxon
pKa (Strongest Basic)-3ChemAxon
Physiological Charge-1ChemAxon
Hydrogen Acceptor Count5ChemAxon
Hydrogen Donor Count4ChemAxon
Polar Surface Area107.22ChemAxon
Rotatable Bond Count2ChemAxon
Refractivity37.03ChemAxon
Polarizability14.94ChemAxon
Spectra
SpectraNot Available
Biological Properties
Cellular Locations
  • Cytoplasm
  • Extracellular
Biofluid Locations
  • Amniotic Fluid
  • Blood
  • Cellular Cytoplasm
  • Cerebrospinal Fluid (CSF)
  • Saliva
  • Urine
Tissue Location
  • Adipose Tissue
  • Adrenal Cortex
  • Adrenal Medulla
  • Bladder
  • Brain
  • Epidermis
  • Erythrocyte
  • Eye Lens
  • Fibroblasts
  • Gonads
  • Heart
  • Intestine
  • Liver
  • Lung
  • Lymphocyte
  • Most Tissues
  • Muscle
  • Myelin
  • Neuron
  • Placenta
  • Platelet
  • Prostate
  • Skeletal Muscle
  • Spleen
Pathways
NameSMPDB LinkKEGG Link
Catecholamine BiosynthesisSMP00012map00350
Normal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
Amniotic FluidDetected and Quantified20.4 +/- 12.21 uMAdult (>18 years old)BothNormal details
BloodDetected and Quantified88.6 (21.0 - 171.0) uMChildren (1-13 years old)Not SpecifiedNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified60.8 +/- 15.9 uMAdult (>18 years old)Not SpecifiedNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified51.0 (11.0 - 125.0) uMNewborn (0-30 days old)Not SpecifiedNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified36.0 +/- 18.0 uMAdult (>18 years old)BothNormal details
BloodDetected and Quantified63.0 (11.0-114.0) uMAdult (>18 years old)BothNormal
    • The Merck Manual,...
details
BloodDetected and Quantified22.2 (14.0-40.0) uMAdult (>18 years old)BothNormal details
BloodDetected and Quantified27.0 (11.1-49.7) uMAdult (>18 years old)MaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified50.9 (35.4-80.1) uMAdult (>18 years old)FemaleNormal
    • Geigy Scientific ...
details
Cellular CytoplasmDetected and Quantified68.0 +/- 43.0 uMAdult (>18 years old)FemaleNormal
    • Geigy Scientific ...
details
Cerebrospinal Fluid (CSF)Detected and Quantified68.0 (17.0-119.0) uMAdult (>18 years old)BothNormal
    • Geigy Scientific ...
details
Cerebrospinal Fluid (CSF)Detected and Quantified163.8 +/- 21 uMAdult (>18 years old)Not SpecifiedNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified133 +/- 58.8 uMAdult (>18 years old)Not SpecifiedNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified164.0 (143.0-185.0) uMAdult (>18 years old)BothNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified144.0 (36.2-251.0) uMAdult (>18 years old)BothNormal details
SalivaDetected and Quantified8.009 +/- 3.959 uMAdult (>18 years old)BothNormal
    • Dame, ZT. et al. ...
details
UrineDetected but not QuantifiedNot ApplicableAdult (>18 years old)Both
Normal
details
UrineDetected and Quantified32.5 (4.6-78) umol/mmol creatinineAdult (>18 years old)Both
Normal
details
UrineDetected and Quantified1.70-22.72 umol/mmol creatinineAdult (>18 years old)BothNormal
    • David F. Putnam C...
details
UrineDetected and Quantified17.0 +/- 2.5 umol/mmol creatinineNewborn (0-30 days old)BothNormal
    • Geigy Scientific ...
details
UrineDetected and Quantified63.6 +/-142.9 umol/mmol creatinineInfant (0-1 year old)BothNormal details
UrineDetected and Quantified0.512 +/-0.058 umol/mmol creatinineAdult (>18 years old)BothNormal details
Abnormal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified39.0 +/- 92.7 uMAdult (>18 years old)Both
Hyperoxalemia
details
BloodDetected and Quantified6.5 +/- 18.6 uMAdult (>18 years old)Both
Hyperoxalemia
details
BloodDetected and Quantified82.57 +/- 36.71 uMAdult (>18 years old)BothCanavan disease details
Cerebrospinal Fluid (CSF)Detected and Quantified53.8 (45.8-61.8) uMChildren (1-13 years old)Both
Brain injury
details
Cerebrospinal Fluid (CSF)Detected and Quantified11.9 (0.0-24) uMAdult (>18 years old)Both
Meningitis
details
Associated Disorders and Diseases
Disease References
Traumatic brain injury
  1. Bayir H, Kagan VE, Tyurina YY, Tyurin V, Ruppel RA, Adelson PD, Graham SH, Janesko K, Clark RS, Kochanek PM: Assessment of antioxidant reserves and oxidative stress in cerebrospinal fluid after severe traumatic brain injury in infants and children. Pediatr Res. 2002 May;51(5):571-8. Pubmed: 11978879
Canavan disease
  1. Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. Pubmed: 16139832
Hyperoxalemia
  1. Ogawa Y, Machida N, Jahana M, Gakiya M, Chinen Y, Oda M, Morozumi M, Sugaya K: Major factors modulating the serum oxalic acid level in hemodialysis patients. Front Biosci. 2004 Sep 1;9:2901-8. Pubmed: 15353324
Meningitis
  1. Kastenbauer S, Koedel U, Becker BF, Pfister HW: Oxidative stress in bacterial meningitis in humans. Neurology. 2002 Jan 22;58(2):186-91. Pubmed: 11805243
Associated OMIM IDs
DrugBank IDDB00126
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDFDB001224
KNApSAcK IDC00001179
Chemspider ID10189562
KEGG Compound IDC00072
BioCyc IDASCORBATE
BiGG ID33747
Wikipedia LinkAscorbic acid
NuGOwiki LinkHMDB00044
Metagene LinkHMDB00044
METLIN ID3753
PubChem Compound54670067
PDB ID1E71
ChEBI ID17208
References
Synthesis ReferenceNot Available
Material Safety Data Sheet (MSDS)Download (PDF)
General References
  1. Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. Pubmed: 19212411
  2. Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. Pubmed: 2026685
  3. Jacobsson L, Lindgarde F, Manthorpe R, Akesson B: Fatty acid composition of adipose tissue and serum micronutrients in relation to common rheumatic complaints in Swedish adults 50-70 years old. Scand J Rheumatol. 1992;21(4):171-7. Pubmed: 1529283
  4. Bayir H, Kagan VE, Tyurina YY, Tyurin V, Ruppel RA, Adelson PD, Graham SH, Janesko K, Clark RS, Kochanek PM: Assessment of antioxidant reserves and oxidative stress in cerebrospinal fluid after severe traumatic brain injury in infants and children. Pediatr Res. 2002 May;51(5):571-8. Pubmed: 11978879
  5. Luck MR, Jeyaseelan I, Scholes RA: Ascorbic acid and fertility. Biol Reprod. 1995 Feb;52(2):262-6. Pubmed: 7711198
  6. Sotiriou S, Gispert S, Cheng J, Wang Y, Chen A, Hoogstraten-Miller S, Miller GF, Kwon O, Levine M, Guttentag SH, Nussbaum RL: Ascorbic-acid transporter Slc23a1 is essential for vitamin C transport into the brain and for perinatal survival. Nat Med. 2002 May;8(5):514-7. Pubmed: 11984597
  7. Wolters M, Hickstein M, Flintermann A, Tewes U, Hahn A: Cognitive performance in relation to vitamin status in healthy elderly German women-the effect of 6-month multivitamin supplementation. Prev Med. 2005 Jul;41(1):253-9. Epub 2005 Jan 6. Pubmed: 15917019
  8. Chiplonkar SA, Agte VV, Tarwadi KV, Paknikar KM, Diwate UP: Micronutrient deficiencies as predisposing factors for hypertension in lacto-vegetarian Indian adults. J Am Coll Nutr. 2004 Jun;23(3):239-47. Pubmed: 15190049
  9. Dudek H, Farbiszewski R, Rydzewska M, Michno T, Kozlowski A: [Concentration of glutathione (GSH), ascorbic acid (vitamin C) and substances reacting with thiobarbituric acid (TBA-rs) in single human brain metastases] Wiad Lek. 2005;58(7-8):379-81. Pubmed: 16425787
  10. Berndt SI, Carter HB, Landis PK, Hallfrisch J, Rohrmann S, Metter EJ, Platz EA: Prediagnostic plasma vitamin C levels and the subsequent risk of prostate cancer. Nutrition. 2005 Jun;21(6):686-90. Pubmed: 15925292
  11. Atanasova BD, Li AC, Bjarnason I, Tzatchev KN, Simpson RJ: Duodenal ascorbate and ferric reductase in human iron deficiency. Am J Clin Nutr. 2005 Jan;81(1):130-3. Pubmed: 15640471
  12. Huang J, May JM: Ascorbic acid protects SH-SY5Y neuroblastoma cells from apoptosis and death induced by beta-amyloid. Brain Res. 2006 Jun 30;1097(1):52-8. Epub 2006 May 24. Pubmed: 16725131
  13. Kastenbauer S, Koedel U, Becker BF, Pfister HW: Oxidative stress in bacterial meningitis in humans. Neurology. 2002 Jan 22;58(2):186-91. Pubmed: 11805243
  14. Hino K, Murakami Y, Nagai A, Kitase A, Hara Y, Furutani T, Ren F, Yamaguchi Y, Yutoku K, Yamashita S, Okuda M, Okita M, Okita K: Alpha-tocopherol [corrected] and ascorbic acid attenuates the ribavirin [corrected] induced decrease of eicosapentaenoic acid in erythrocyte membrane in chronic hepatitis C patients. J Gastroenterol Hepatol. 2006 Aug;21(8):1269-75. Pubmed: 16872308
  15. Kodama M, Inoue F, Kodama T, Kodama M: Intraperitoneal administration of ascorbic acid delays the turnover of 3H-labelled cortisol in the plasma of an ODS rat, but not in the Wistar rat. Evidence in support of the cardinal role of vitamin C in the progression of glucocorticoid synthesis. In Vivo. 1996 Jan-Feb;10(1):97-102. Pubmed: 8726814
  16. Trommer H, Bottcher R, Poppl A, Hoentsch J, Wartewig S, Neubert RH: Role of ascorbic acid in stratum corneum lipid models exposed to UV irradiation. Pharm Res. 2002 Jul;19(7):982-90. Pubmed: 12180551
  17. Grunewald RA: Ascorbic acid in the brain. Brain Res Brain Res Rev. 1993 Jan-Apr;18(1):123-33. Pubmed: 8467348
  18. Close GL, Ashton T, Cable T, Doran D, Holloway C, McArdle F, MacLaren DP: Ascorbic acid supplementation does not attenuate post-exercise muscle soreness following muscle-damaging exercise but may delay the recovery process. Br J Nutr. 2006 May;95(5):976-81. Pubmed: 16611389
  19. Li C, Chen Y, Wang Q: [Whole bladder wall laser irradiation to prevent bladder cancer recurrence with intravesical HpD and ascorbic acid] Zhonghua Zhong Liu Za Zhi. 1997 Nov;19(6):463-5. Pubmed: 10920885
  20. Wannamethee SG, Lowe GD, Rumley A, Bruckdorfer KR, Whincup PH: Associations of vitamin C status, fruit and vegetable intakes, and markers of inflammation and hemostasis. Am J Clin Nutr. 2006 Mar;83(3):567-74; quiz 726-7. Pubmed: 16522902
  21. Padayatty SJ, Levine M: Vitamin C and myocardial infarction: the heart of the matter. Am J Clin Nutr. 2000 May;71(5):1027-8. Pubmed: 10799361
  22. Englard S, Seifter S: The biochemical functions of ascorbic acid. Annu Rev Nutr. 1986;6:365-406. Pubmed: 3015170
  23. Proctor P: Similar functions of uric acid and ascorbate in man? Nature. 1970 Nov 28;228(5274):868. Pubmed: 5477017
  24. Meister A: Glutathione-ascorbic acid antioxidant system in animals. J Biol Chem. 1994 Apr 1;269(13):9397-400. Pubmed: 8144521
  25. Banhegyi G, Mandl J: The hepatic glycogenoreticular system. Pathol Oncol Res. 2001;7(2):107-10. Pubmed: 11458272
  26. Padayatty SJ, Katz A, Wang Y, Eck P, Kwon O, Lee JH, Chen S, Corpe C, Dutta A, Dutta SK, Levine M: Vitamin C as an antioxidant: evaluation of its role in disease prevention. J Am Coll Nutr. 2003 Feb;22(1):18-35. Pubmed: 12569111
  27. Korcok J, Dixon SJ, Lo TC, Wilson JX: Differential effects of glucose on dehydroascorbic acid transport and intracellular ascorbate accumulation in astrocytes and skeletal myocytes. Brain Res. 2003 Dec 12;993(1-2):201-7. Pubmed: 14642847

Enzymes

General function:
Involved in monooxygenase activity
Specific function:
Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
Gene Name:
PAM
Uniprot ID:
P19021
Molecular weight:
108402.425
Reactions
Peptidylglycine + Ascorbic acid + Oxygen → peptidyl(2-hydroxyglycine) + Dehydroascorbic acid + Waterdetails
References
  1. Romero I, Teresa Sanchez-Ballesta M, Maldonado R, Isabel Escribano M, Merodio C: Anthocyanin, antioxidant activity and stress-induced gene expression in high CO2-treated table grapes stored at low temperature. J Plant Physiol. 2008;165(5):522-30. Epub 2007 Jun 13. Pubmed: 17570561
  2. Floryszak-Wieczorek J, Milczarek G, Arasimowicz M, Ciszewski A: Do nitric oxide donors mimic endogenous NO-related response in plants? Planta. 2006 Nov;224(6):1363-72. Epub 2006 Jun 14. Pubmed: 16773376
  3. Crespo A, Marti MA, Roitberg AE, Amzel LM, Estrin DA: The catalytic mechanism of peptidylglycine alpha-hydroxylating monooxygenase investigated by computer simulation. J Am Chem Soc. 2006 Oct 4;128(39):12817-28. Pubmed: 17002377
General function:
Involved in monooxygenase activity
Specific function:
Conversion of dopamine to noradrenaline.
Gene Name:
DBH
Uniprot ID:
P09172
Molecular weight:
69064.45
Reactions
Dopamine + Ascorbic acid + Oxygen → xi-Norepinephrine + Dehydroascorbic acid + Waterdetails
Dopamine + Ascorbic acid + Oxygen → Norepinephrine + Dehydroascorbic acid + Waterdetails
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
  3. Suzuki E, Kurata T, Shibata M, Mori M, Arakawa N: Activities of D- and L-xyloascorbic acid and D- and L-araboascorbic acid as a cofactor for dopamine beta-hydroxylase reaction. J Nutr Sci Vitaminol (Tokyo). 1997 Oct;43(5):491-6. Pubmed: 9505234
  4. Pettingill TM, Strange RW, Blackburn NJ: Carbonmonoxy dopamine beta-hydroxylase. Structural characterization by Fourier transform infrared, fluorescence, and x-ray absorption spectroscopy. J Biol Chem. 1991 Sep 15;266(26):16996-7003. Pubmed: 1894598
  5. Feng J, Shi J, Sirimanne SR, Mounier-Lee CE, May SW: Kinetic and stereochemical studies on novel inactivators of C-terminal amidation. Biochem J. 2000 Sep 1;350 Pt 2:521-30. Pubmed: 10947967
General function:
Involved in electron carrier activity
Specific function:
Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.
Gene Name:
PHYH
Uniprot ID:
O14832
Molecular weight:
38538.065
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Gene Name:
P4HA2
Uniprot ID:
O15460
Molecular weight:
60632.19
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Gene Name:
P4HA1
Uniprot ID:
P13674
Molecular weight:
60966.645
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
General function:
Involved in hydrolase activity, hydrolyzing O-glycosyl compounds
Specific function:
LPH splits lactose in the small intestine.
Gene Name:
LCT
Uniprot ID:
P09848
Molecular weight:
218584.77
References
  1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed: 10592235
General function:
Involved in iron ion binding
Specific function:
Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
Gene Name:
BBOX1
Uniprot ID:
O75936
Molecular weight:
44714.6
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
  3. Dunn WA, Rettura G, Seifter E, Englard S: Carnitine biosynthesis from gamma-butyrobetaine and from exogenous protein-bound 6-N-trimethyl-L-lysine by the perfused guinea pig liver. Effect of ascorbate deficiency on the in situ activity of gamma-butyrobetaine hydroxylase. J Biol Chem. 1984 Sep 10;259(17):10764-70. Pubmed: 6432788
  4. Vaz FM, van Gool S, Ofman R, IJlst L, Wanders RJ: Carnitine biosynthesis. Purification of gamma-butyrobetaine hydroxylase from rat liver. Adv Exp Med Biol. 1999;466:117-24. Pubmed: 10709635
  5. Rebouche CJ: Ascorbic acid and carnitine biosynthesis. Am J Clin Nutr. 1991 Dec;54(6 Suppl):1147S-1152S. Pubmed: 1962562
General function:
Involved in oxidoreductase activity
Specific function:
Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.
Gene Name:
PLOD1
Uniprot ID:
Q02809
Molecular weight:
83549.55
References
  1. Myllyla R, Majamaa K, Gunzler V, Hanauske-Abel HM, Kivirikko KI: Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase. J Biol Chem. 1984 May 10;259(9):5403-5. Pubmed: 6325436
  2. Salavoura K, Valari M, Kolialexi A, Mavrou A, Kitsiou S: A case of Ehlers Danlos syndrome type VI. Genet Couns. 2006;17(3):291-4. Pubmed: 17100196
  3. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. Pubmed: 11752352
General function:
Involved in oxidoreductase activity
Specific function:
Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.
Gene Name:
PLOD2
Uniprot ID:
O00469
Molecular weight:
84685.07
References
  1. Myllyla R, Majamaa K, Gunzler V, Hanauske-Abel HM, Kivirikko KI: Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase. J Biol Chem. 1984 May 10;259(9):5403-5. Pubmed: 6325436
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  3. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
General function:
Involved in oxidoreductase activity
Specific function:
Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.
Gene Name:
PLOD3
Uniprot ID:
O60568
Molecular weight:
84784.505
References
  1. Myllyla R, Majamaa K, Gunzler V, Hanauske-Abel HM, Kivirikko KI: Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase. J Biol Chem. 1984 May 10;259(9):5403-5. Pubmed: 6325436
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  3. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
General function:
Involved in glutathione transferase activity
Specific function:
Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid.
Gene Name:
GSTO1
Uniprot ID:
P78417
Molecular weight:
27565.6
Reactions
Glutathione + Dehydroascorbic acid → Oxidized glutathione + Ascorbic aciddetails
General function:
Involved in glutathione transferase activity
Specific function:
Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA).
Gene Name:
GSTO2
Uniprot ID:
Q9H4Y5
Molecular weight:
24399.09
Reactions
Glutathione + Dehydroascorbic acid → Oxidized glutathione + Ascorbic aciddetails
General function:
Involved in isomerase activity
Specific function:
This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP
Gene Name:
P4HB
Uniprot ID:
P07237
Molecular weight:
57115.8
General function:
Involved in transporter activity
Specific function:
Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate
Gene Name:
SLC23A1
Uniprot ID:
Q9UHI7
Molecular weight:
64830.4
References
  1. Kang JS, Kim HN, Jung da J, Kim JE, Mun GH, Kim YS, Cho D, Shin DH, Hwang YI, Lee WJ: Regulation of UVB-induced IL-8 and MCP-1 production in skin keratinocytes by increasing vitamin C uptake via the redistribution of SVCT-1 from the cytosol to the membrane. J Invest Dermatol. 2007 Mar;127(3):698-706. Epub 2006 Sep 28. Pubmed: 17008880
  2. Johnston L, Laverty G: Vitamin C transport and SVCT1 transporter expression in chick renal proximal tubule cells in culture. Comp Biochem Physiol A Mol Integr Physiol. 2007 Mar;146(3):327-34. Epub 2006 Dec 5. Pubmed: 17258485
  3. Savini I, Rossi A, Pierro C, Avigliano L, Catani MV: SVCT1 and SVCT2: key proteins for vitamin C uptake. Amino Acids. 2008 Apr;34(3):347-55. Epub 2007 Jun 1. Pubmed: 17541511
  4. Perez MJ, Castano B, Gonzalez-Buitrago JM, Marin JJ: Multiple protective effects of melatonin against maternal cholestasis-induced oxidative stress and apoptosis in the rat fetal liver-placenta-maternal liver trio. J Pineal Res. 2007 Sep;43(2):130-9. Pubmed: 17645691
  5. Steiling H, Longet K, Moodycliffe A, Mansourian R, Bertschy E, Smola H, Mauch C, Williamson G: Sodium-dependent vitamin C transporter isoforms in skin: Distribution, kinetics, and effect of UVB-induced oxidative stress. Free Radic Biol Med. 2007 Sep 1;43(5):752-62. Epub 2007 May 10. Pubmed: 17664139
General function:
Nucleotide transport and metabolism
Specific function:
Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate
Gene Name:
SLC23A2
Uniprot ID:
Q9UGH3
Molecular weight:
70336.2
General function:
Involved in oxidation reduction
Specific function:
Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML).
Gene Name:
TMLHE
Uniprot ID:
Q9NVH6
Molecular weight:
44048.895
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
General function:
Involved in oxidoreductase activity
Specific function:
Dioxygenase that repairs alkylated DNA and RNA containing 1-methyladenine and 3-methylcytosine by oxidative demethylation. Can also repair alkylated DNA containing 1-ethenoadenine (in vitro). Has strong preference for double-stranded DNA. Has low efficiency with single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron.
Gene Name:
ALKBH2
Uniprot ID:
Q6NS38
Molecular weight:
29322.22
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
General function:
Involved in oxidoreductase activity
Specific function:
Dioxygenase that repairs alkylated DNA containing 1- methyladenine and 3-methylcytosine by oxidative demethylation. Has a strong preference for single-stranded DNA. May also act on RNA. Requires molecular oxygen, alpha-ketoglutarate and iron
Gene Name:
ALKBH3
Uniprot ID:
Q96Q83
Molecular weight:
33374.5
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
General function:
Involved in oxidoreductase activity
Specific function:
Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts.
Gene Name:
LEPRE1
Uniprot ID:
Q32P28
Molecular weight:
78921.41
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
General function:
Involved in oxidoreductase activity
Specific function:
Shows prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly-sequences in collagens, especially types II, IV and V (By similarity).
Gene Name:
LEPREL1
Uniprot ID:
Q8IVL5
Molecular weight:
60386.32
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
General function:
Involved in iron ion binding
Specific function:
Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly-sequences in collagens, especially types IV and V (By similarity).
Gene Name:
LEPREL2
Uniprot ID:
Q8IVL6
Molecular weight:
81835.705
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
General function:
Involved in transporter activity
Specific function:
Not Available
Gene Name:
SLC23A3
Uniprot ID:
Q6PIS1
Molecular weight:
64529.9
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Gene Name:
P4HA3
Uniprot ID:
Q7Z4N8
Molecular weight:
61125.675
General function:
Involved in oxidoreductase activity
Specific function:
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality.
Gene Name:
EGLN1
Uniprot ID:
Q9GZT9
Molecular weight:
46020.585
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
General function:
Involved in oxidoreductase activity
Specific function:
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle. Also regulates susceptibility to normoxic oxidative neuronal death.
Gene Name:
EGLN2
Uniprot ID:
Q96KS0
Molecular weight:
43650.03
References
  1. Nytko KJ, Spielmann P, Camenisch G, Wenger RH, Stiehl DP: Regulated function of the prolyl-4-hydroxylase domain (PHD) oxygen sensor proteins. Antioxid Redox Signal. 2007 Sep;9(9):1329-38. Pubmed: 17627474
  2. Bruegge K, Jelkmann W, Metzen E: Hydroxylation of hypoxia-inducible transcription factors and chemical compounds targeting the HIF-alpha hydroxylases. Curr Med Chem. 2007;14(17):1853-62. Pubmed: 17627521
General function:
Involved in oxidoreductase activity
Specific function:
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Also hydroxylates PKM in hypoxia, limiting glycolysis. Under normoxia, hydroxylates and regulates the stability of ADRB2. Regulator of cardiomyocyte and neuronal apoptosis. In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex. In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity. Also essential for hypoxic regulation of neutrophilic inflammation. Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway.
Gene Name:
EGLN3
Uniprot ID:
Q9H6Z9
Molecular weight:
27261.06
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
General function:
Involved in calcium ion binding
Specific function:
Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex.
Gene Name:
P4HTM
Uniprot ID:
Q9NXG6
Molecular weight:
63111.98
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
General function:
Involved in iron ion binding
Specific function:
Not Available
Gene Name:
OGFOD1
Uniprot ID:
Q8N543
Molecular weight:
63245.7
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
General function:
Involved in iron ion binding
Specific function:
Not Available
Gene Name:
OGFOD2
Uniprot ID:
Q6N063
Molecular weight:
38996.1
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423