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Human Metabolome Database Version 2.5

 

Showing metabocard for Prostaglandin F2a (HMDB01139)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-06-02 16:23:22
Accession Number HMDB01139
Secondary Accession Numbers Not Available
Common Name Prostaglandin F2a
Description Prostaglandin F2a (PGF2) is one of the earliest discovered and most common prostaglandins. It is actively biosynthesized in various organs of mammals and exhibits a variety of biological activities, including contraction of pulmonary arteries. It is used in medicine to induce labor and as an abortifacient. PGF2a binds to the Prostaglandin F2 receptor (PTGFR) which is a member of the G-protein coupled receptor family. PGF2-alpha mediates luteolysis. Luteolysis is the structural and functional degradation of the corpus luteum (CL) that occurs at the end of the luteal phase of both the estrous and menstrual cycles in the absence of pregnancy. PGF2 may also be involved in modulating intraocular pressure and smooth muscle contraction in the uterus and gastrointestinal tract sphincters. PGF2 is mainly synthesized directly from PGH2 by PGH2 9,11-endoperoxide reductase. A small amount of PGF2 is also produced from PGE2 by PGE2 9-ketoreductase. A PGF2 epimer has been reported to exhibit various biological activities, and its levels are increased in bronchoalveolar lavage fluid, plasma, and urine in patients with mastocytosis and bronchial asthma. PGF2 is synthesized from PGD2 by PGD2 11-ketoreductase. (PMID: 16475787) Prostaglandins are eicosanoids. The eicosanoids consist of the prostaglandins (PGs), thromboxanes (TXs), leukotrienes (LTs) and lipoxins (LXs). The PGs and TXs are collectively identified as prostanoids. Prostaglandins were originally shown to be synthesized in the prostate gland, thromboxanes from platelets (thrombocytes) and leukotrienes from leukocytes, hence the derivation of their names. All mammalian cells except erythrocytes synthesize eicosanoids. These molecules are extremely potent, able to cause profound physiological effects at very dilute concentrations. All eicosanoids function locally at the site of synthesis, through receptor-mediated G-protein linked signaling pathways.
Synonyms
  1. Protamodin
  2. Prostin F 2 alpha
  3. Prostarmon F
  4. Prostamate
  5. Prostaglandin F2a
  6. Prostaglandin F2
  7. Panacelan
  8. PGF2a
  9. Glandin N
  10. Enzaprost F
  11. Enzaprost
  12. Dinoprost
  13. Dinifertin
  14. Cyclosin
  15. Amoglandin
  16. 9a,11a-PGF2a
  17. 9a,11a-PGF2
  18. 9a,11a,15(S)-Trihydroxy-5-cis-13-trans-prostadienoic acid
  19. 7-[3,5-dihydroxy-2-(3-hydroxy-1-octenyl)cyclopentyl]-5-Heptenoic acid
  20. (5Z,9a,11a,13E,15S)-9,11,15-trihydroxy-Prosta-5,13-dien-1-oic acid
  21. (+)-Prostaglandin F2a
  22. (5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoate
  23. (5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoic acid
  24. (5Z,13E,15S)-9a,11a,15-trihydroxyprosta-5,13-dien-1-oic acid
  25. (5Z,13E,15S)-9a,11a,15-trihydroxyprosta-5,13-dien-1-oate
  26. 7-[3,5-Dihydroxy-2-(3-hydroxy-1-octenyl)cyclopentyl]-5-heptenoate
  27. 9,11,15-Trihydroxy-(5Z,9a,11a,13E,15S)-prosta-5,13-dien-1-oic acid
  28. 9,11,15-Trihydroxy-(5Z,9a,11a,13E,15S)-prosta-5,13-dien-1-oate
  29. l-Prostaglandin F2-alpha
  30. l-PGF2-alpha
  31. 9a,11a,15(S)-Trihydroxy-5-cis-13-trans-prostadienoate
  32. (5Z,9a,11a,13E,15S)-9,11,15-trihydroxy-Prosta-5,13-dien-1-oate
  33. 9,11,15-trihydroxyprosta-5Z,13E-dien-1-oate
  34. (9alpha,11alpha,15)-trihydroxyprosta-(5Z,13E)-dien-1-oic acid
  35. F2a Isoprostane
  36. 9,11,15-trihydroxyprosta-5Z,13E-dien-1-oic acid
  37. (9alpha,11alpha,15)-trihydroxyprosta-(5Z,13E)-dien-1-oate
Chemical IUPAC Name 7-[(1R,2S,3R,5R)-3,5-dihydroxy-2-[(3S)-3-hydroxyoct-1-enyl]cyclopentyl]hept-5-enoic acid
Chemical Formula C20H34O5
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Prostanoids
Sub Class
  • Prostaglandins
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • carboxylic acid
  • alkene
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 354.481
Monoisotopic Molecular Weight 354.240631
Isomeric SMILES CCCCC[C@H](O)C=C[C@H]1[C@H](O)C[C@H](O)[C@@H]1CC=CCCCC(O)=O
Canonical SMILES CCCCCC(O)C=CC1C(O)CC(O)C1CC=CCCCC(O)=O
KEGG Compound ID C00639 Link Image
BioCyc ID 5Z13E-15S-9-ALPHA11-ALPHA15-TRIHY Link Image
BiGG ID 35568 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01139 Link Image
Metagene Link HMDB01139 Link Image
METLIN ID 6032 Link Image
PubChem Compound 11081 Link Image
PubChem Substance 10628789 Link Image
ChEBI ID 15553 Link Image
CAS Registry Number 551-11-1
InChI Identifier InChI=1/C20H34O5/c1-2-3-6-9-15(21)12-13-17-16(18(22)14-19(17)23)10-7-4-5-8-11-20(24)25/h4,7,12-13,15-19,21-23H,2-3,5-6,8-11,14H2,1H3,(H,24,25)/b7-4+,13-12+/t15-,16+,17+,18-,19+/m0/s1
Synthesis Reference Chen, Shaoqing; Janda, Kim D. Total synthesis of naturally occurring prostaglandin F2a on a non-crosslinked polystyrene support. Tetrahedron Letters (1998), 39(23), 3943-3946.
Melting Point (Experimental) 30 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.00258 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 0.117 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity 4.39 [BODOR,H & HUANG,M (1992)] Source: PhysProp
Predicted LogP/Hydrophobicity 3.2 [Predicted by PubChem via XLOGP]; 3.11 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • Extracellular
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Adipose Tissue —
Adrenal Gland —
Epidermis —
Placenta —
Platelet —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 0.000371 +/- 0.000144 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Oxygenated lipids were quantified by Theresa L. Pedersen and John W. Newman at the USDA’s Western Human Nutrition Research Center, Davis, CA, and Lipomics Technologies, Inc.
References
  • Psychogios N, Hau DD, Peng J, Guo AC, Mandal R, Bouatra S, Sinelnikov I, Krishnamurthy R, Eisner R, Gautam B, Young N, Xia J, Knox C, Dong E, Huang P, Hollander Z, Pedersen TL, Smith SR, Bamforth F, Greiner R, McManus B, Newman JW, Goodfriend T, Wishart DS: The human serum metabolome. PLoS One. 2011 Feb 16;6(2):e16957. [PubMed Link Image]
  • Wishart DS, Knox C, Guo AC, Eisner R, Young N, Gautam B, Hau DD, Psychogios N, Dong E, Bouatra S, Mandal R, Sinelnikov I, Xia J, Jia L, Cruz JA, Lim E, Sobsey CA, Shrivastava S, Huang P, Liu P, Fang L, Peng J, Fradette R, Cheng D, Tzur D, Clements M, Lewis A, De Souza A, Zuniga A, Dawe M, Xiong Y, Clive D, Greiner R, Nazyrova A, Shaykhutdinov R, Li L, Vogel HJ, Forsythe I: HMDB: a knowledgebase for the human metabolome. Nucleic Acids Res. 2008 Oct 25. [PubMed Link Image]
Biofluid Blood
Value 5.3E-5 +/- 1.2E-5 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Quehenberger O, Armando AM, Brown AH, Milne SB, Myers DS, Merrill AH, Bandyopadhyay S, Jones KN, Kelly S, Shaner RL, Sullards CM, Wang E, Murphy RC, Barkley RM, Leiker TJ, Raetz CR, Guan Z, Laird GM, Six DA, Russell DW, McDonald JG, Subramaniam S, Fahy E, Dennis EA: Lipidomics reveals a remarkable diversity of lipids in human plasma. J Lipid Res. 2010 Nov;51(11):3299-305. Epub 2010 Jul 29. [PubMed Link Image]
Biofluid CSF
Value 0.002 (0.0-0.004) 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.
Biofluid CSF
Value 0.00091 +/- 0.00008 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Measured via MS/MS techniques from 4 pooled CSF samples provided by TNO/NuGO – The Netherlands
References
  • John W. Newman, USDA ARS Western Human Nutrition Research Center, Davis CA (personal communication - March 2, 2009)
Biofluid CSF
Value 7.340e-05 +/- 8.469e-06 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal (control)
Comments Not Available
References
  • Romero SD, Chyatte D, Byer DE, Romero JC, Yaksh TL: Measurement of prostaglandins in the cerebrospinal fluid in cat, dog, and man. J Neurochem. 1984 Dec;43(6):1642-9. [PubMed Link Image]
Biofluid CSF
Value 0.000500 (0.000452-0.000545) uM
Age N/A
Sex N/A
Patient information HIV-Seropositive (Neurologically normal)
Comments Not Available
References
  • Griffin DE, Wesselingh SL, McArthur JC: Elevated central nervous system prostaglandins in human immunodeficiency virus-associated dementia. Ann Neurol. 1994 May;35(5):592-7. [PubMed Link Image]
Biofluid CSF
Value 7.340e-05 +/- 8.469e-06 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Romero SD, Chyatte D, Byer DE, Romero JC, Yaksh TL: Measurement of prostaglandins in the cerebrospinal fluid in cat, dog, and man. J Neurochem. 1984 Dec;43(6):1642-9. [PubMed Link Image]
Biofluid Urine
Value 0.0000924 (0.0000588-0.000126) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Ciabattoni G, Pugliese F, Spaldi M, Cinotti GA, Patrono C: Radioimmunoassay measurement of prostaglandins E2 and F2alpha in human urine. J Endocrinol Invest. 1979 Apr-Jun;2(2):173-82. [PubMed Link Image]
Biofluid Urine
Value 0.00021 +/- 0.000053 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 0.00031 +/- 0.00012 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Concentrations (Abnormal)
Biofluid Blood
Value 0.0010 +/- 0.0002 uM
Age Adult:>18 yrs old
Sex Both
Condition Cardiac arrest
Comments Patients with out-of-hospital cardiac arrest (resuscitated with cardiopulmonary resuscitation), age range of 39 to 87 years old, n=15
References
  • Strohmenger HU, Lindner KH, Keller A, Lindner IM, Bothner U, Georgieff M: Concentrations of prolactin and prostaglandins during and after cardiopulmonary resuscitation. Crit Care Med. 1995 Aug;23(8):1347-55. [PubMed Link Image]
Biofluid Blood
Value 0.0005 +/- 0.0001 uM
Age Adult:>18 yrs old
Sex Both
Condition Cardiac arrest
Comments Patients with out-of-hospital cardiac arrest (nonresuscitated with cardiopulmonary resuscitation), age range of 39 to 87 years old, n=14
References
  • Strohmenger HU, Lindner KH, Keller A, Lindner IM, Bothner U, Georgieff M: Concentrations of prolactin and prostaglandins during and after cardiopulmonary resuscitation. Crit Care Med. 1995 Aug;23(8):1347-55. [PubMed Link Image]
Biofluid Blood
Value 0.0016 +/- 0.0004 uM
Age Adult:>18 yrs old
Sex Both
Condition Cardiac arrest
Comments Patients with out-of-hospital cardiac arrest (resuscitated with cardiopulmonary resuscitation and discharged), age range of 39 to 87 years old
References
  • Strohmenger HU, Lindner KH, Keller A, Lindner IM, Bothner U, Georgieff M: Concentrations of prolactin and prostaglandins during and after cardiopulmonary resuscitation. Crit Care Med. 1995 Aug;23(8):1347-55. [PubMed Link Image]
Biofluid Blood
Value 0.0007 +/- 0.0001 uM
Age Adult:>18 yrs old
Sex Both
Condition Cardiac arrest
Comments Patients with out-of-hospital cardiac arrest (resuscitated with cardiopulmonary resuscitation and nondischarged), age range of 39 to 87 years old
References
  • Strohmenger HU, Lindner KH, Keller A, Lindner IM, Bothner U, Georgieff M: Concentrations of prolactin and prostaglandins during and after cardiopulmonary resuscitation. Crit Care Med. 1995 Aug;23(8):1347-55. [PubMed Link Image]
Biofluid CSF
Value 0.000545 (4.799e-05-0.00192) uM
Age N/A
Sex N/A
Comments Not Available
References
  • Griffin DE, Wesselingh SL, McArthur JC: Elevated central nervous system prostaglandins in human immunodeficiency virus-associated dementia. Ann Neurol. 1994 May;35(5):592-7. [PubMed Link Image]
Associated Disorders
Condition References
Cardiac arrest
  • Strohmenger HU, Lindner KH, Keller A, Lindner IM, Bothner U, Georgieff M: Concentrations of prolactin and prostaglandins during and after cardiopulmonary resuscitation. Crit Care Med. 1995 Aug;23(8):1347-55. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Arachidonic Acid Metabolism SMP00075 Link Image map00590 Link Image
General References
  1. Grinsted J, Byskov AG: Meiosis-inducing and meiosis-preventing substances in human male reproductive organs. Fertil Steril. 1981 Feb;35(2):199-204. [PubMed Link Image]
  2. Catanzarite VA: Prophylactic intramyometrial carboprost tromethamine does not substantially reduce blood loss relative to intramyometrial oxytocin at routine cesarean section. Am J Perinatol. 1990 Jan;7(1):39-42. [PubMed Link Image]
  3. Carr BR, Milburn J Jr, Wright EE, Simpson ER: Adenylate cyclase activity in neocortex and fetal zone membrane fractions of the human fetal adrenal gland. J Clin Endocrinol Metab. 1985 Apr;60(4):718-22. [PubMed Link Image]
  4. Negrel R, Gaillard D, Ailhaud G: Prostacyclin as a potent effector of adipose-cell differentiation. Biochem J. 1989 Jan 15;257(2):399-405. [PubMed Link Image]
  5. Hammarstrom S, Hamberg M, Samuelsson B, Duell EA, Stawiski M, Voorhees JJ: Increased concentrations of nonesterified arachidonic acid, 12L-hydroxy-5,8,10,14-eicosatetraenoic acid, prostaglandin E2, and prostaglandin F2alpha in epidermis of psoriasis. Proc Natl Acad Sci U S A. 1975 Dec;72(12):5130-4. [PubMed Link Image]
  6. Steele GL, Leung PC: Intragonadal signalling mechanisms in the control of steroid hormone production. J Steroid Biochem Mol Biol. 1992 Mar;41(3-8):515-22. [PubMed Link Image]
  7. Ciabattoni G, Pugliese F, Spaldi M, Cinotti GA, Patrono C: Radioimmunoassay measurement of prostaglandins E2 and F2alpha in human urine. J Endocrinol Invest. 1979 Apr-Jun;2(2):173-82. [PubMed Link Image]
  8. Davi G, Chiarelli F, Santilli F, Pomilio M, Vigneri S, Falco A, Basili S, Ciabattoni G, Patrono C: Enhanced lipid peroxidation and platelet activation in the early phase of type 1 diabetes mellitus: role of interleukin-6 and disease duration. Circulation. 2003 Jul 1;107(25):3199-203. Epub 2003 Jun 16. [PubMed Link Image]
Metabolic Enzymes
  1. Carbonyl reductase [NADPH] 1
  2. Carbonyl reductase [NADPH] 3
  3. 15-hydroxyprostaglandin dehydrogenase [NAD+]
  4. cDNA, FLJ95780, Homo sapiens carbonyl reductase 1 (CBR1), mRNA (Carbonyl reductase 1, isoform CRA_d)
Enzyme 1 [top]
Enzyme 1 ID 5304
Enzyme 1 Name Carbonyl reductase [NADPH] 1
Enzyme 1 Synonyms
  1. 15-hydroxyprostaglandin dehydrogenase [NADP+]
  2. NADPH-dependent carbonyl reductase 1
  3. Prostaglandin 9-ketoreductase
  4. Prostaglandin-E(2) 9-reductase
Enzyme 1 Gene Name CBR1
Enzyme 1 Protein Sequence >Carbonyl reductase [NADPH] 1 
MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFH
QLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRD
VCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTK
KGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKA
TKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW
Enzyme 1 Number of Residues 277
Enzyme 1 Molecular Weight 30374.7
Enzyme 1 Theoretical pI 8.49
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 1 General Function Involved in oxidoreductase activity
Enzyme 1 Specific Function NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NADP+ = (13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate + NADPH + H+ [RN:R04552]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID P16152 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name CBR1_HUMAN Link Image
Enzyme 1 PDB ID 1WMA Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >834 bp 
ATGTCGTCCGGCATCCATGTAGCGCTGGTGACTGGAGGCAACAAGGGCATCGGCTTGGCC
ATCGTGCGCGACCTGTGCCGGCTGTTCTCGGGGGACGTGGTGCTCACGGCGCGGGACGTG
ACGCGGGGCCAGGCGGCCGTACAGCAGCTGCAGGCGGAGGGCCTGAGCCCGCGCTTCCAC
CAGCTGGACATCGACGATCTGCAGAGCATCCGCGCCCTGCGCGACTTCCTGCGCAAGGAG
TACGGGGGCCTGGACGTGCTGGTCAACAACGCGGGCATCGCCTTCAAGGTTGCTGATCCC
ACACCCTTTCATATTCAAGCTGAAGTGACGATGAAAACAAATTTCTTTGGTACCCGAGAT
GTGTGCACAGAATTACTCCCTCTAATAAAACCCCAAGGGAGAGTGGTGAACGTATCTAGC
ATCATGAGCGTCAGAGCCCTTAAAAGCTGCAGCCCAGAGCTGCAGCAGAAGTTCCGCAGT
GAGACCATCACTGAGGAGGAGCTGGTGGGGCTCATGAACAAGTTTGTGGAGGATACAAAG
AAGGGAGTGCACCAGAAGGAGGGCTGGCCCAGCAGCGCATACGGGGTGACGAAGATTGGC
GTCACCGTTCTGTCCAGGATCCACGCCAGGAAACTGAGTGAGCAGAGGAAAGGGGACAAG
ATCCTCCTGAATGCCTGCTGCCCAGGGTGGGTGAGAACTGACATGGCGGGACCCAAGGCC
ACCAAGAGCCCAGAAGAAGGTGCAGAGACCCCTGTGTACTTGGCCCTTTTGCCCCCAGAT
GCTGAGGGTCCCCATGGACAATTTGTTTCAGAGAAGAGAGTTGAACAGTGGTGA
Enzyme 1 GenBank Gene ID J04056 Link Image
Enzyme 1 GeneCard ID CBR1 Link Image
Enzyme 1 GenAtlas ID CBR1 Link Image
Enzyme 1 HGNC ID HGNC:1548 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 21q22.13
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Wermuth B, Bohren KM, Heinemann G, von Wartburg JP, Gabbay KH: Human carbonyl reductase. Nucleotide sequence analysis of a cDNA and amino acid sequence of the encoded protein. J Biol Chem. 1988 Nov 5;263(31):16185-8. [PubMed Link Image]
  2. Forrest GL, Akman S, Krutzik S, Paxton RJ, Sparkes RS, Doroshow J, Felsted RL, Glover CJ, Mohandas T, Bachur NR: Induction of a human carbonyl reductase gene located on chromosome 21. Biochim Biophys Acta. 1990 Apr 6;1048(2-3):149-55. [PubMed Link Image]
  3. Forrest GL, Akman S, Doroshow J, Rivera H, Kaplan WD: Genomic sequence and expression of a cloned human carbonyl reductase gene with daunorubicin reductase activity. Mol Pharmacol. 1991 Oct;40(4):502-7. [PubMed Link Image]
  4. Watanabe K, Sugawara C, Ono A, Fukuzumi Y, Itakura S, Yamazaki M, Tashiro H, Osoegawa K, Soeda E, Nomura T: Mapping of a novel human carbonyl reductase, CBR3, and ribosomal pseudogenes to human chromosome 21q22.2. Genomics. 1998 Aug 15;52(1):95-100. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Krook M, Ghosh D, Stromberg R, Carlquist M, Jornvall H: Carboxyethyllysine in a protein: native carbonyl reductase/NADP(+)-dependent prostaglandin dehydrogenase. Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):502-6. [PubMed Link Image]
  9. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  10. Gonzalez-Covarrubias V, Kalabus JL, Blanco JG: Inhibition of polymorphic human carbonyl reductase 1 (CBR1) by the cardioprotectant flavonoid 7-monohydroxyethyl rutoside (monoHER). Pharm Res. 2008 Jul;25(7):1730-4. Epub 2008 May 1. [PubMed Link Image]
  11. Tanaka M, Bateman R, Rauh D, Vaisberg E, Ramachandani S, Zhang C, Hansen KC, Burlingame AL, Trautman JK, Shokat KM, Adams CL: An unbiased cell morphology-based screen for new, biologically active small molecules. PLoS Biol. 2005 May;3(5):e128. Epub 2005 Apr 5. [PubMed Link Image]
  12. Bateman R, Rauh D, Shokat KM: Glutathione traps formaldehyde by formation of a bicyclo[4.4.1]undecane adduct. Org Biomol Chem. 2007 Oct 21;5(20):3363-7. Epub 2007 Aug 29. [PubMed Link Image]
  13. Bateman RL, Rauh D, Tavshanjian B, Shokat KM: Human carbonyl reductase 1 is an S-nitrosoglutathione reductase. J Biol Chem. 2008 Dec 19;283(51):35756-62. Epub 2008 Sep 29. [PubMed Link Image]
  14. Gonzalez-Covarrubias V, Ghosh D, Lakhman SS, Pendyala L, Blanco JG: A functional genetic polymorphism on human carbonyl reductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH binding affinity. Drug Metab Dispos. 2007 Jun;35(6):973-80. Epub 2007 Mar 7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5306
Enzyme 2 Name Carbonyl reductase [NADPH] 3
Enzyme 2 Synonyms
  1. NADPH-dependent carbonyl reductase 3
Enzyme 2 Gene Name CBR3
Enzyme 2 Protein Sequence >Carbonyl reductase [NADPH] 3 
MSSCSRVALVTGANRGIGLAIARELCRQFSGDVVLTARDVARGQAAVQQLQAEGLSPRFH
QLDIDDLQSIRALRDFLRKEYGGLNVLVNNAAVAFKSDDPMPFDIKAEMTLKTNFFATRN
MCNELLPIMKPHGRVVNISSLQCLRAFENCSEDLQERFHSETLTEGDLVDLMKKFVEDTK
NEVHEREGWPNSPYGVSKLGVTVLSRILARRLDEKRKADRILVNACCPGPVKTDMDGKDS
IRTVEEGAETPVYLALLPPDATEPQGQLVHDKVVQNW
Enzyme 2 Number of Residues 277
Enzyme 2 Molecular Weight 30850.0
Enzyme 2 Theoretical pI 6.06
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 2 General Function Involved in oxidoreductase activity
Enzyme 2 Specific Function Has low NADPH-dependent oxidoreductase activity towards 4-benzoylpyridine and menadione (in vitro)
Enzyme 2 Pathways
Enzyme 2 Reactions
  • R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+ [RN:R03557]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 3702679 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O75828 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CBR3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >834 bp 
ATGTCGTCCGGCATCCATGTAGCGCTGGTGACTGGAGGCAACAAGGGCATCGGCTTGGCC
ATCGTGCGCGACCTGTGCCGGCTGTTCTCGGGGGACGTGGTGCTCACGGCGCGGGACGTG
ACGCGGGGCCAGGCGGCCGTACAGCAGCTGCAGGCGGAGGGCCTGAGCCCGCGCTTCCAC
CAGCTGGACATCGACGATCTGCAGAGCATCCGCGCCCTGCGCGACTTCCTGCGCAAGGAG
TACGGGGGCCTGGACGTGCTGGTCAACAACGCGGGCATCGCCTTCAAGGTTGCTGATCCC
ACACCCTTTCATATTCAAGCTGAAGTGACGATGAAAACAAATTTCTTTGGTACCCGAGAT
GTGTGCACAGAATTACTCCCTCTAATAAAACCCCAAGGGAGAGTGGTGAACGTATCTAGC
ATCATGAGCGTCAGAGCCCTTAAAAGCTGCAGCCCAGAGCTGCAGCAGAAGTTCCGCAGT
GAGACCATCACTGAGGAGGAGCTGGTGGGGCTCATGAACAAGTTTGTGGAGGATACAAAG
AAGGGAGTGCACCAGAAGGAGGGCTGGCCCAGCAGCGCATACGGGGTGACGAAGATTGGC
GTCACCGTTCTGTCCAGGATCCACGCCAGGAAACTGAGTGAGCAGAGGAAAGGGGACAAG
ATCCTCCTGAATGCCTGCTGCCCAGGGTGGGTGAGAACTGACATGGCGGGACCCAAGGCC
ACCAAGAGCCCAGAAGAAGGTGCAGAGACCCCTGTGTACTTGGCCCTTTTGCCCCCAGAT
GCTGAGGGTCCCCATGGACAATTTGTTTCAGAGAAGAGAGTTGAACAGTGGTGA
Enzyme 2 GenBank Gene ID AB003151 Link Image
Enzyme 2 GeneCard ID CBR3 Link Image
Enzyme 2 GenAtlas ID CBR3 Link Image
Enzyme 2 HGNC ID HGNC:1549 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 21q22.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Watanabe K, Sugawara C, Ono A, Fukuzumi Y, Itakura S, Yamazaki M, Tashiro H, Osoegawa K, Soeda E, Nomura T: Mapping of a novel human carbonyl reductase, CBR3, and ribosomal pseudogenes to human chromosome 21q22.2. Genomics. 1998 Aug 15;52(1):95-100. [PubMed Link Image]
  2. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Miura T, Nishinaka T, Terada T: Different functions between human monomeric carbonyl reductase 3 and carbonyl reductase 1. Mol Cell Biochem. 2008 Aug;315(1-2):113-21. Epub 2008 May 21. [PubMed Link Image]
  5. Lakhman SS, Ghosh D, Blanco JG: Functional significance of a natural allelic variant of human carbonyl reductase 3 (CBR3). Drug Metab Dispos. 2005 Feb;33(2):254-7. Epub 2004 Nov 10. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5307
Enzyme 3 Name 15-hydroxyprostaglandin dehydrogenase [NAD+]
Enzyme 3 Synonyms
  1. 15-PGDH
  2. Prostaglandin dehydrogenase 1
Enzyme 3 Gene Name HPGD
Enzyme 3 Protein Sequence >15-hydroxyprostaglandin dehydrogenase [NAD+] 
MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLF
IQCDVADQQQLRDTFRKVVDHFGRLDILVNNAGVNNEKNWEKTLQINLVSVISGTYLGLD
YMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASKHGIVGFTRSAALAANLMNSGVRLNA
ICPGFVNTAILESIEKEENMGQYIEYKDHIKDMIKYYGILDPPLIANGLITLIEDDALNG
AIMKITTSKGIHFQDYDTTPFQAKTQ
Enzyme 3 Number of Residues 266
Enzyme 3 Molecular Weight 28977.1
Enzyme 3 Theoretical pI 5.65
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 3 General Function Involved in oxidoreductase activity
Enzyme 3 Specific Function Prostaglandin inactivation. Contributes to the regulation of events that are under the control of prostaglandin levels. Catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4. Inhibits in vivo proliferation of colon cancer cells
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • (5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+ [RN:R02580]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 189054417 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P15428 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PGDH_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >801 bp 
ATGCACGTGAACGGCAAAGTGGCGCTGGTGACCGGCGCGGCTCAGGGCATAGGCAGAGCC
TTTGCAGAGGCGCTGCTGCTTAAGGGCGCCAAGGTAGCGCTGGTGGATTGGAATCTTGAA
GCAGGTGTACAGTGTAAAGCTGCCCTGGATGAGCAGTTTGAACCTCAGAAGACTCTGTTC
ATCCAGTGCGATGTGGCTGACCAGCAACAACTGAGAGACACTTTTAGAAAAGTTGTAGAC
CACTTTGGAAGACTGGACATTTTGGTCAATAATGCTGGAGTGAATAATGAGAAAAACTGG
GAAAAAACTCTGCAAATTAATTTGGTTTCTGTTATCAGTGGAACCTATCTTGGTTTGGAT
TACATGAGTAAGCAAAATGGAGGTGAAGGCGGCATCATTATCAATATGTCATCTTTAGCA
GGACTCATGCCCGTTGCACAGCAGCCGGTTTATTGTGCTTCAAAGCATGGCATAGTTGGA
TTCACACGCTCAGCAGCGTTGGCTGCTAATCTTATGAACAGTGGTGTGAGACTGAATGCC
ATTTGTCCAGGCTTTGTTAACACAGCCATCCTTGAATCAATTGAAAAAGAAGAAAACATG
GGACAATATATAGAATATAAGGATCATATCAAGGATATGATTAAATACTATGGAATTTTG
GACCCACCATTGATTGCCAATGGATTGATAACACTCATTGAAGATGATGCTTTAAATGGT
GCTATTATGAAGATCACAACTTCTAAGGGAATTCATTTTCAAGACTATGATACAACTCCA
TTTCAAGCAAAAACCCAATGA
Enzyme 3 GenBank Gene ID AK314624 Link Image
Enzyme 3 GeneCard ID HPGD Link Image
Enzyme 3 GenAtlas ID HPGD Link Image
Enzyme 3 HGNC ID HGNC:5154 Link Image
Enzyme 3 Chromosome Location 4
Enzyme 3 Locus 4q34-q35
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Krook M, Marekov L, Jornvall H: Purification and structural characterization of placental NAD(+)-linked 15-hydroxyprostaglandin dehydrogenase. The primary structure reveals the enzyme to belong to the short-chain alcohol dehydrogenase family. Biochemistry. 1990 Jan 23;29(3):738-43. [PubMed Link Image]
  2. Ensor CM, Yang JY, Okita RT, Tai HH: Cloning and sequence analysis of the cDNA for human placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase. J Biol Chem. 1990 Sep 5;265(25):14888-91. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Ensor CM, Tai HH: Site-directed mutagenesis of the conserved tyrosine 151 of human placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme. Biochem Biophys Res Commun. 1991 Apr 30;176(2):840-5. [PubMed Link Image]
  6. Clish CB, Levy BD, Chiang N, Tai HH, Serhan CN: Oxidoreductases in lipoxin A4 metabolic inactivation: a novel role for 15-onoprostaglandin 13-reductase/leukotriene B4 12-hydroxydehydrogenase in inflammation. J Biol Chem. 2000 Aug 18;275(33):25372-80. [PubMed Link Image]
  7. Patel FA, Funder JW, Challis JR: Mechanism of cortisol/progesterone antagonism in the regulation of 15-hydroxyprostaglandin dehydrogenase activity and messenger ribonucleic acid levels in human chorion and placental trophoblast cells at term. J Clin Endocrinol Metab. 2003 Jun;88(6):2922-33. [PubMed Link Image]
  8. Yan M, Rerko RM, Platzer P, Dawson D, Willis J, Tong M, Lawrence E, Lutterbaugh J, Lu S, Willson JK, Luo G, Hensold J, Tai HH, Wilson K, Markowitz SD: 15-Hydroxyprostaglandin dehydrogenase, a COX-2 oncogene antagonist, is a TGF-beta-induced suppressor of human gastrointestinal cancers. Proc Natl Acad Sci U S A. 2004 Dec 14;101(50):17468-73. Epub 2004 Dec 1. [PubMed Link Image]
  9. Cho H, Huang L, Hamza A, Gao D, Zhan CG, Tai HH: Role of glutamine 148 of human 15-hydroxyprostaglandin dehydrogenase in catalytic oxidation of prostaglandin E2. Bioorg Med Chem. 2006 Oct 1;14(19):6486-91. Epub 2006 Jul 7. [PubMed Link Image]
  10. Krook M, Ghosh D, Duax W, Jornvall H: Three-dimensional model of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase and relationships to the NADP(+)-dependent enzyme (carbonyl reductase). FEBS Lett. 1993 May 10;322(2):139-42. [PubMed Link Image]
  11. Uppal S, Diggle CP, Carr IM, Fishwick CW, Ahmed M, Ibrahim GH, Helliwell PS, Latos-Bielenska A, Phillips SE, Markham AF, Bennett CP, Bonthron DT: Mutations in 15-hydroxyprostaglandin dehydrogenase cause primary hypertrophic osteoarthropathy. Nat Genet. 2008 Jun;40(6):789-93. Epub 2008 May 25. [PubMed Link Image]
  12. Tariq M, Azeem Z, Ali G, Chishti MS, Ahmad W: Mutation in the HPGD gene encoding NAD+ dependent 15-hydroxyprostaglandin dehydrogenase underlies isolated congenital nail clubbing (ICNC). J Med Genet. 2009 Jan;46(1):14-20. Epub 2008 Sep 19. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 12989
Enzyme 4 Name cDNA, FLJ95780, Homo sapiens carbonyl reductase 1 (CBR1), mRNA (Carbonyl reductase 1, isoform CRA_d)
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name CBR1
Enzyme 4 Protein Sequence >cDNA, FLJ95780, Homo sapiens carbonyl reductase 1 (CBR1) 
MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFH
QLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRD
VCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTK
KGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKA
TKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW
Enzyme 4 Number of Residues 277
Enzyme 4 Molecular Weight 30375
Enzyme 4 Theoretical pI Not Available
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function Not Available
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID B2RBZ7 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name B2RBZ7_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID Not Available
Enzyme 4 GeneCard ID B2RBZ7 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available