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Human Metabolome Database Version 2.5

 

Showing metabocard for Glyceraldehyde (HMDB01051)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-04 15:33:48
Accession Number HMDB01051
Secondary Accession Numbers Not Available
Common Name Glyceraldehyde
Description Glyceraldehyde is a triose monosaccharide with chemical formula C3H6O3. It is the simplest of all common aldoses. It is a sweet colorless crystalline solid that is an intermediate compound in carbohydrate metabolism. The word comes from combining glycerine and aldehyde, as glyceraldehyde is merely glycerine with one hydroxide changed to an aldehyde.
Synonyms
  1. (+/-)-2,3-dihydroxy-Propanal
  2. (+/-)-Glyceraldehyde
  3. 2,3-Dihydroxypropanal
  4. 2,3-Dihydroxypropionaldehyde
  5. D-(+)-Glyceraldehyde
  6. D-2,3-dihydroxypropanal
  7. D-2,3-dihydroxypropionaldehyde
  8. D-Glyceraldehyde
  9. D-aldotriose
  10. D-glycerose
  11. DL-Glyceraldehyde
  12. Dihydroxypropionaldehyde
  13. Glyceraldehyde
  14. Glyceric aldehyde
  15. Glycerinaldehyde
  16. Glycerinformal
  17. Glycerose
  18. alpha,beta-Dihydroxypropionaldehyde
  19. delta-(+)-Glyceraldehyde
  20. delta-2,3-dihydroxypropanal
  21. delta-2,3-dihydroxypropionaldehyde
  22. delta-Glyceraldehyde
  23. delta-aldotriose
  24. delta-glycerose
Chemical IUPAC Name 2,3-dihydroxypropanal
Chemical Formula C3H6O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Alcohols and Polyols
Sub Class
  • Simple alcohols
Family
  • Mammalian Metabolite
Species
  • aldehyde
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
Biofunction
  • Component of Fructose and mannose metabolism
  • Component of Inositol metabolism
Application
Source
  • Endogenous
Average Molecular Weight 90.078
Monoisotopic Molecular Weight 90.031693
Isomeric SMILES OCC(O)C=O
Canonical SMILES OCC(O)C=O
KEGG Compound ID C02154 Link Image
BioCyc ID GLYCERALD Link Image
BiGG ID 35402 Link Image
Wikipedia Link Glyceraldehyde Link Image
NuGOwiki Link HMDB01051 Link Image
Metagene Link HMDB01051 Link Image
METLIN ID 4176 Link Image
PubChem Compound 751 Link Image
PubChem Substance 10520413 Link Image
ChEBI ID 5445 Link Image
CAS Registry Number 56-82-6
InChI Identifier InChI=1/C3H6O3/c4-1-3(6)2-5/h1,3,5-6H,2H2
Synthesis Reference Wan, Xin-Jun; Song, Ming-You; Wu, Rong; Chu, Dao-Bao. Synthesis of glyceraldehyde by indirect electrooxidation. Yingyong Huaxue (2003), 20(6), 578-581.
Melting Point (Experimental) 145 oC
Experimental Water Solubility 17 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 195.0 mg/mL [MEYLAN,WM et al. (1996)]; 814.00006 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.63 [Predicted by ALOGPS]; -1.3 [Predicted by PubChem via XLOGP]; -1.07 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID 1W3T 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 Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from Solubility)
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
Neuron
Concentrations (Normal)
Biofluid Blood
Value 1476.0 +/- 655.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Jonas AJ, Lin SN, Conley SB, Schneider JA, Williams JC, Caprioli RC: Urine glyceraldehyde excretion is elevated in the renal Fanconi syndrome. Kidney Int. 1989 Jan;35(1):99-104. [PubMed Link Image]
Biofluid Urine
Value 50.00 +/- 50.00 umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Jonas AJ, Lin SN, Conley SB, Schneider JA, Williams JC, Caprioli RC: Urine glyceraldehyde excretion is elevated in the renal Fanconi syndrome. Kidney Int. 1989 Jan;35(1):99-104. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Urine
Value 6407.7 +/- 6030.8 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Fanconi syndrome
Comments Not Available
References
  • Jonas AJ, Lin SN, Conley SB, Schneider JA, Williams JC, Caprioli RC: Urine glyceraldehyde excretion is elevated in the renal Fanconi syndrome. Kidney Int. 1989 Jan;35(1):99-104. [PubMed Link Image]
Associated Disorders
Condition References
Fanconi syndrome
  • Jonas AJ, Lin SN, Conley SB, Schneider JA, Williams JC, Caprioli RC: Urine glyceraldehyde excretion is elevated in the renal Fanconi syndrome. Kidney Int. 1989 Jan;35(1):99-104. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Glycerolipid Metabolism SMP00039 Link Image map00561 Link Image
General References
  1. Gugliucci A: A practical method to study functional impairment of proteins by glycation and effects of inhibitors using current coagulation/fibrinolysis reagent kits. Clin Biochem. 2003 Mar;36(2):155-8. [PubMed Link Image]
  2. Beard KM, Shangari N, Wu B, O'Brien PJ: Metabolism, not autoxidation, plays a role in alpha-oxoaldehyde- and reducing sugar-induced erythrocyte GSH depletion: relevance for diabetes mellitus. Mol Cell Biochem. 2003 Oct;252(1-2):331-8. [PubMed Link Image]
  3. Iwata H, Ukeda H, Maruyama T, Fujino T, Sawamura M: Effect of carbonyl compounds on red blood cells deformability. Biochem Biophys Res Commun. 2004 Aug 27;321(3):700-6. [PubMed Link Image]
  4. Zakrzewska I, Prokopowicz J, Worowski K, Skrzydlewska E, Puchalski Z, Piotrowski Z: Low molecular organic inactivators in differentiating organ origin of alpha-amylase in humans. Part I. Mater Med Pol. 1989 Oct-Dec;21(4):274-6. [PubMed Link Image]
  5. Phillipou G, Seaborn CJ, Phillips PJ: Re-evaluation of the fructosamine reaction. Clin Chem. 1988 Aug;34(8):1561-4. [PubMed Link Image]
  6. Fujita T, Funako T, Hayashi H: 8-Hydroxydaidzein, an aldose reductase inhibitor from okara fermented with Aspergillus sp. HK-388. Biosci Biotechnol Biochem. 2004 Jul;68(7):1588-90. [PubMed Link Image]
  7. Haraguchi H, Hayashi R, Ishizu T, Yagi A: A flavone from Manilkara indica as a specific inhibitor against aldose reductase in vitro. Planta Med. 2003 Sep;69(9):853-5. [PubMed Link Image]
  8. Yamagishi S, Nakamura K, Inoue H, Kikuchi S, Takeuchi M: Serum or cerebrospinal fluid levels of glyceraldehyde-derived advanced glycation end products (AGEs) may be a promising biomarker for early detection of Alzheimer's disease. Med Hypotheses. 2005;64(6):1205-7. [PubMed Link Image]
  9. Choei H, Sasaki N, Takeuchi M, Yoshida T, Ukai W, Yamagishi S, Kikuchi S, Saito T: Glyceraldehyde-derived advanced glycation end products in Alzheimer's disease. Acta Neuropathol (Berl). 2004 Sep;108(3):189-93. Epub 2004 Jun 17. [PubMed Link Image]
  10. Jonas AJ, Lin SN, Conley SB, Schneider JA, Williams JC, Caprioli RC: Urine glyceraldehyde excretion is elevated in the renal Fanconi syndrome. Kidney Int. 1989 Jan;35(1):99-104. [PubMed Link Image]
  11. Takeuchi M, Yamagishi S: Alternative routes for the formation of glyceraldehyde-derived AGEs (TAGE) in vivo. Med Hypotheses. 2004;63(3):453-5. [PubMed Link Image]
  12. Nagaraj RH, Oya-Ito T, Padayatti PS, Kumar R, Mehta S, West K, Levison B, Sun J, Crabb JW, Padival AK: Enhancement of chaperone function of alpha-crystallin by methylglyoxal modification. Biochemistry. 2003 Sep 16;42(36):10746-55. [PubMed Link Image]
  13. Wikipedia Link Image
Metabolic Enzymes
  1. Aldose reductase
  2. Aldehyde dehydrogenase, mitochondrial
  3. Alcohol dehydrogenase [NADP+]
Enzyme 1 [top]
Enzyme 1 ID 5320
Enzyme 1 Name Aldose reductase
Enzyme 1 Synonyms
  1. AR
  2. Aldehyde reductase
  3. Aldo-keto reductase family 1 member B1
Enzyme 1 Gene Name AKR1B1
Enzyme 1 Protein Sequence >Aldose reductase
MASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQ
EKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGK
EFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKP
AVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAK
HNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCA
LLSCTSHKDYPFHEEF
Enzyme 1 Number of Residues 316
Enzyme 1 Molecular Weight 35853.1
Enzyme 1 Theoretical pI 6.99
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 1 General Function Involved in oxidoreductase activity
Enzyme 1 Specific Function Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies
Enzyme 1 Pathways
Enzyme 1 Reactions
  • alditol + NAD(P)+ = aldose + NAD(P)H + H+ [RN:R02819 R02820]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 2687578 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P15121 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ALDR_HUMAN Link Image
Enzyme 1 PDB ID 1T40 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >951 bp
ATGGCAAGCCGTCTCCTGCTCAACAACGGCGCCAAGATGCCCATCCTGGGGTTGGGTACC
TGGAAGTCCCCTCCAGGGCAGGTGACTGAGGCCGTGAAGGTGGCCATTGACGTCGGGTAC
CGCCACATCGACTGTGCCCATGTGTACCAGAATGAGAATGAGGTGGGGGTGGCCATTCAG
GAGAAGCTCAGGGAGCAGGTGGTGAAGCGTGAGGAGCTCTTCATCGTCAGCAAGCTGTGG
TGCACGTACCATGAGAAGGGCCTGGTGAAAGGAGCCTGCCAGAAGACACTCAGCGACCTG
AAGCTGGACTACCTGGACCTCTACCTTATTCACTGGCCGACTGGCTTTAAGCCTGGGAAG
GAATTTTTCCCATTGGATGAGTCGGGCAATGTGGTTCCCAGTGACACCAACATTCTGGAC
ACGTGGGCGGCCATGGAAGAGCTGGTGGATGAAGGGCTGGTGAAAGCTATTGGCATCTCC
AACTTCAACCATCTCCAGGTGGAGATGATCTTAAACAAACCTGGCTTGAAGTATAAGCCT
GCAGTTAACCAGATTGAGTGCCACCCATATCTCACTCAGGAGAAGTTAATCCAGTACTGC
CAGTCCAAAGGCATCGTGGTGACCGCCTACAGCCCCCTCGGCTCTCCTGACAGGCCCTGG
GCCAAGCCCGAGGACCCTTCTCTCCTGGAGGATCCCAGGATCAAGGCGATCGCAGCCAAG
CACAATAAAACTACAGCCCAGGTCCTGATCCGGTTCCCCATGCAGAGGAACTTGGTGGTG
ATCCCCAAGTCTGTGACACCAGAACGCATTGCTGAGAACTTTAAGGTCTTTGACTTTGAA
CTGAGCAGCCAGGATATGACCACCTTACTCAGCTACAACAGGAACTGGAGGGTCTGTGCC
TTGTTGAGCTGTACCTCCCACAAGGATTACCCCTTCCATGAAGAGTTTTGA
Enzyme 1 GenBank Gene ID AF032455 Link Image
Enzyme 1 GeneCard ID AKR1B1 Link Image
Enzyme 1 GenAtlas ID AKR1B1 Link Image
Enzyme 1 HGNC ID HGNC:381 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7q35
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Bohren KM, Bullock B, Wermuth B, Gabbay KH: The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J Biol Chem. 1989 Jun 5;264(16):9547-51. [PubMed Link Image]
  2. Chung S, LaMendola J: Cloning and sequence determination of human placental aldose reductase gene. J Biol Chem. 1989 Sep 5;264(25):14775-7. [PubMed Link Image]
  3. Graham A, Hedge PJ, Powell SJ, Riley J, Brown L, Gammack A, Carey F, Markham AF: Nucleotide sequence of cDNA for human aldose reductase. Nucleic Acids Res. 1989 Oct 25;17(20):8368. [PubMed Link Image]
  4. Grundmann U, Bohn H, Obermeier R, Amann E: Cloning and prokaryotic expression of a biologically active human placental aldose reductase. DNA Cell Biol. 1990 Apr;9(3):149-57. [PubMed Link Image]
  5. Nishimura C, Matsuura Y, Kokai Y, Akera T, Carper D, Morjana N, Lyons C, Flynn TG: Cloning and expression of human aldose reductase. J Biol Chem. 1990 Jun 15;265(17):9788-92. [PubMed Link Image]
  6. Graham A, Brown L, Hedge PJ, Gammack AJ, Markham AF: Structure of the human aldose reductase gene. J Biol Chem. 1991 Apr 15;266(11):6872-7. [PubMed Link Image]
  7. Ko BC, Ruepp B, Bohren KM, Gabbay KH, Chung SS: Identification and characterization of multiple osmotic response sequences in the human aldose reductase gene. J Biol Chem. 1997 Jun 27;272(26):16431-7. [PubMed Link Image]
  8. Hartmann TB, Thiel D, Dummer R, Schadendorf D, Eichmuller S: SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma. Br J Dermatol. 2004 Feb;150(2):252-8. [PubMed Link Image]
  9. 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]
  10. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  11. 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]
  12. Ferraretto A, Negri A, Giuliani A, De Grada L, Fuhrman Conti AM, Ronchi S: Aldose reductase is involved in long-term adaptation of EUE cells to hyperosmotic stress. Biochim Biophys Acta. 1993 Feb 17;1175(3):283-8. [PubMed Link Image]
  13. Morjana NA, Lyons C, Flynn TG: Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine. J Biol Chem. 1989 Feb 15;264(5):2912-9. [PubMed Link Image]
  14. Liu SQ, Bhatnagar A, Ansari NH, Srivastava SK: Identification of the reactive cysteine residue in human placenta aldose reductase. Biochim Biophys Acta. 1993 Aug 7;1164(3):268-72. [PubMed Link Image]
  15. Jaquinod M, Potier N, Klarskov K, Reymann JM, Sorokine O, Kieffer S, Barth P, Andriantomanga V, Biellmann JF, Van Dorsselaer A: Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes. Eur J Biochem. 1993 Dec 15;218(3):893-903. [PubMed Link Image]
  16. Tarle I, Borhani DW, Wilson DK, Quiocho FA, Petrash JM: Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110. J Biol Chem. 1993 Dec 5;268(34):25687-93. [PubMed Link Image]
  17. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  18. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  19. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  20. Wilson DK, Bohren KM, Gabbay KH, Quiocho FA: An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science. 1992 Jul 3;257(5066):81-4. [PubMed Link Image]
  21. Borhani DW, Harter TM, Petrash JM: The crystal structure of the aldose reductase.NADPH binary complex. J Biol Chem. 1992 Dec 5;267(34):24841-7. [PubMed Link Image]
  22. Wilson DK, Tarle I, Petrash JM, Quiocho FA: Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat. Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):9847-51. [PubMed Link Image]
  23. Harrison DH, Bohren KM, Petsko GA, Ringe D, Gabbay KH: The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant. Biochemistry. 1997 Dec 23;36(51):16134-40. [PubMed Link Image]
  24. Ruiz F, Hazemann I, Mitschler A, Joachimiak A, Schneider T, Karplus M, Podjarny A: The crystallographic structure of the aldose reductase-IDD552 complex shows direct proton donation from tyrosine 48. Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1347-54. Epub 2004 Jul 21. [PubMed Link Image]
  25. Howard EI, Sanishvili R, Cachau RE, Mitschler A, Chevrier B, Barth P, Lamour V, Van Zandt M, Sibley E, Bon C, Moras D, Schneider TR, Joachimiak A, Podjarny A: Ultrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 A. Proteins. 2004 Jun 1;55(4):792-804. [PubMed Link Image]
  26. Steuber H, Zentgraf M, Podjarny A, Heine A, Klebe G: High-resolution crystal structure of aldose reductase complexed with the novel sulfonyl-pyridazinone inhibitor exhibiting an alternative active site anchoring group. J Mol Biol. 2006 Feb 10;356(1):45-56. Epub 2005 Nov 10. [PubMed Link Image]
  27. Biadene M, Hazemann I, Cousido A, Ginell S, Joachimiak A, Sheldrick GM, Podjarny A, Schneider TR: The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop. Acta Crystallogr D Biol Crystallogr. 2007 Jun;63(Pt 6):665-72. Epub 2007 May 15. [PubMed Link Image]
  28. Steuber H, Zentgraf M, La Motta C, Sartini S, Heine A, Klebe G: Evidence for a novel binding site conformer of aldose reductase in ligand-bound state. J Mol Biol. 2007 May 25;369(1):186-97. Epub 2007 Mar 15. [PubMed Link Image]
  29. Steuber H, Heine A, Klebe G: Structural and thermodynamic study on aldose reductase: nitro-substituted inhibitors with strong enthalpic binding contribution. J Mol Biol. 2007 May 4;368(3):618-38. Epub 2006 Dec 15. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5530
Enzyme 2 Name Aldehyde dehydrogenase, mitochondrial
Enzyme 2 Synonyms
  1. ALDH class 2
  2. ALDH-E2
  3. ALDHI
Enzyme 2 Gene Name ALDH2
Enzyme 2 Protein Sequence >Aldehyde dehydrogenase, mitochondrial
MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPS
TGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLA
ALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCG
QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPG
FGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADM
DWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGP
QVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGP
VMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS
PFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
Enzyme 2 Number of Residues 517
Enzyme 2 Molecular Weight 56380.9
Enzyme 2 Theoretical pI 7.05
Enzyme 2 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 2 General Function Involved in oxidoreductase activity
Enzyme 2 Specific Function An aldehyde + NAD(+) + H(2)O = an acid + NADH
Enzyme 2 Pathways
Enzyme 2 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+ [RN:R00538]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 28606 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P05091 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ALDH2_HUMAN Link Image
Enzyme 2 PDB ID 1OF7 Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1551 bp
ATGTTGCGCGCTGCCGCCGCTCGGGCCCCGCCTGGCCGCCGCCTCTTGTCAGCCGCCGCC
ACCCAGGCCGTGCCTGCCCCCAACCAGCAGCCCGAGGTCTTCTGCAACCAGATTTTCATA
AACAATGAATGGCACGATGCCGTCAGCAGGAAAACATTCCCCACCGTCAATCCGTCCACT
GGAGAGGTCATCTGTCAGGTAGCTGAAGGGGACAAGGAAGATGTGGACAAGGCACGTGAA
GGCCGCCCGGGCGCCTTCCAGCTGGGCTCACCTTGGCGCCGCATGGACGCATCACACAGC
GGCCGGCTGCTGAACCGCCTGGCCGATCTGATCGAGCGGGACCGGACCTACCTGGCGGCC
TTGGAGACCCTGGACAATGGCAAGCCCTATGTCATCTCCTACCTGGTGGATTTGGACATG
GTCCTCAAATGTCTCCGGTATTATGCCGGCTGGGCTGATAAGTACCACGGGAAAACCATC
CCCATTGACGGAGACTTCTTCAGCTACACACGCCATGAACCTGTGGGGGTGTGCGGGCAG
ATCATTCCGTGGAATTTCCCGCTCCTGATGCAAGCATGGAAGCTGGGCCCAGCCTTGGCA
ACTGGAAACGTGGTTGTGATGAAGGTAGCTGAGCAGACACCCCTCACCGCCCTCTATGTG
GCCAACCTGATCAAGGAGGCTGGCTTTCCCCCTGGTGTGGTCAACATTGTGCCTGGATTT
GGCCCCACGGCTGGGGCCGCCATTGCCTCCCATGAGGATGTGGACAAAGTGGCATTCACA
GGCTCCACTGAGATTGGCCGCGTAATCCAGGTTGCTGCTGGGAGCAGCAACCTCAAGAGA
GTGACCTTGGAGCTGGGGGGGAAGAGCCCCAACATCATCATGTCAGATGCCGATATGGAT
TGGGCCGTGGAACAGGCCCACTTCGCCCTGTTCTTCAACCAGGGCCAGTGCTGCTGTGCC
GGCTCCCGGACCTTCGTGCAGGAGGACATCTATGATGAGTTTGTGGTGCGGAGCGTTGCC
CGGGCCAAGTCTCGGGTGGTCGGGAACCCCTTTGATAGCAAGACCGAGCAGGGGCCGCAG
GTGGATGAAACTCAGTTTAAGAAGATCCTCGGCTACATCAACACGGGGAAGCAAGAGGGG
GCGAAGCTGCTGTGTGGTGGGGGCATTGCTGCTGACCGTGGTTACTTCATCCAGCCCACT
GTGTTTGGAGATGTGCAGGATGGCATGACCATCGCCAAGGAGGAGATCTTCGGGCCAGTG
ATGCAGATCCTGAAGTTCAAGACCATAGAGGAGGTTGTTGGGAGAGCCAACAATTCCACG
TACGGGCTGGCCGCAGCTGTCTTCACAAAGGATTTGGACAAGGCCAATTACCTGTCCCAG
GCCCTCCAGGCGGGCACTGTGTGGGTCAACTGCTATGATGTGTTTGGAGCCCAGTCACCC
TTTGGTGGCTACAAGATGTCGGGGAGTGGCCGGGAGTTGGGCGAGTACGGGCTGCAGGCA
TACACTGAAGTGAAAACTGTCACAGTCAAAGTGCCTCAGAAGAACTCATAA
Enzyme 2 GenBank Gene ID X05409 Link Image
Enzyme 2 GeneCard ID ALDH2 Link Image
Enzyme 2 GenAtlas ID ALDH2 Link Image
Enzyme 2 HGNC ID HGNC:404 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 12q24.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Evidence for a signal peptide at the amino-terminal end of human mitochondrial aldehyde dehydrogenase. FEBS Lett. 1987 May 11;215(2):233-6. [PubMed Link Image]
  2. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Isolation and sequence analysis of a full length cDNA clone coding for human mitochondrial aldehyde dehydrogenase. Nucleic Acids Res. 1987 Apr 10;15(7):3179. [PubMed Link Image]
  3. Hsu LC, Bendel RE, Yoshida A: Genomic structure of the human mitochondrial aldehyde dehydrogenase gene. Genomics. 1988 Jan;2(1):57-65. [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. Hempel J, Kaiser R, Jornvall H: Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations. Eur J Biochem. 1985 Nov 15;153(1):13-28. [PubMed Link Image]
  6. Hsu LC, Tani K, Fujiyoshi T, Kurachi K, Yoshida A: Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3771-5. [PubMed Link Image]
  7. Yoshida A, Ikawa M, Hsu LC, Tani K: Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases. Alcohol. 1985 Jan-Feb;2(1):103-6. [PubMed Link Image]
  8. Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed Link Image]
  9. Agarwal DP, Goedde HW: Human aldehyde dehydrogenase isozymes and alcohol sensitivity. Isozymes Curr Top Biol Med Res. 1987;16:21-48. [PubMed Link Image]
  10. Hempel J, Hoog JO, Jornvall H: Mitochondrial aldehyde dehydrogenase. Homology of putative targeting sequence to that of carbamyl phosphate synthetase I revealed by correlation of cDNA and protein data. FEBS Lett. 1987 Sep 28;222(1):95-8. [PubMed Link Image]
  11. Ni L, Zhou J, Hurley TD, Weiner H: Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms. Protein Sci. 1999 Dec;8(12):2784-90. [PubMed Link Image]
  12. Yoshida A, Huang IY, Ikawa M: Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals. Proc Natl Acad Sci U S A. 1984 Jan;81(1):258-61. [PubMed Link Image]
  13. Novoradovsky A, Tsai SJ, Goldfarb L, Peterson R, Long JC, Goldman D: Mitochondrial aldehyde dehydrogenase polymorphism in Asian and American Indian populations: detection of new ALDH2 alleles. Alcohol Clin Exp Res. 1995 Oct;19(5):1105-10. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5754
Enzyme 3 Name Alcohol dehydrogenase [NADP+]
Enzyme 3 Synonyms
  1. Aldehyde reductase
  2. Aldo-keto reductase family 1 member A1
Enzyme 3 Gene Name AKR1A1
Enzyme 3 Protein Sequence >Alcohol dehydrogenase [NADP+]
MAASCVLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEAL
KEDVGPGKAVPREELFVTSKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFER
GDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDILSVASVRP
AVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDPDEPVLLEEPVVLALAEK
YGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIV
PMLTVDGKRVPRDAGHPLYPFNDPY
Enzyme 3 Number of Residues 325
Enzyme 3 Molecular Weight 36572.7
Enzyme 3 Theoretical pI 6.79
Enzyme 3 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 3 General Function Involved in oxidoreductase activity
Enzyme 3 Specific Function Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. In vitro substrates include succinic semialdehyde, 4- nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D- glucuronic acid. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN)
Enzyme 3 Pathways
Enzyme 3 Reactions
  • an alcohol + NADP+ = an aldehyde + NADPH + H+ [RN:R07328]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID P14550 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name AK1A1_HUMAN Link Image
Enzyme 3 PDB ID 2ALR Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >978 bp
ATGGCGGCTTCCTGTGTTCTACTGCACACTGGGCAGAAGATGCCTCTGATTGGTCTGGGT
ACCTGGAAGAGTGAGCCTGGTCAGGTAAAAGCAGCTGTTAAGTATGCCCTTAGCGTAGGC
TACCGCCACATTGATTGTGCTGCTATCTACGGCAATGAGCCTGAGATTGGGGAGGCCCTG
AAGGAGGACGTGGGACCAGGCAAGGCGGTGCCTCGGGAGGAGCTGTTTGTGACATCCAAG
CTGTGGAACACCAAGCACCACCCCGAGGATGTGGAGCCTGCCCTCCGGAAGACTCTGGCT
GACCTCCAGCTGGAGTATCTGGACCTGTACCTGATGCACTGGCCTTATGCCTTTGAGCGG
GGAGACAACCCCTTCCCCAAGAATGCTGATGGGACTATATGCTACGACTCCACCCACTAC
AAGGAGACTTGGAAGGCTCTGGAGGCACTGGTGGCTAAGGGGCTGGTGCAGGCGCTGGGC
CTGTCCAACTTCAACAGTCGGCAGATTGATGACATACTCAGTGTGGCCTCCGTGCGTCCA
GCTGTCTTGCAGGTGGAATGCCACCCATACTTGGCTCAAAATGAGCTAATTGCCCACTGC
CAAGCACGTGGCTTGGAGGTAACTGCTTATAGCCCTTTGGGCTCCTCTGATCGTGCATGG
CGTGATCCTGATGAGCCTGTCCTGCTGGAGGAACCAGTAGTCCTGGCATTGGCTGAAAAG
TATGGCCGATCTCCAGCTCAGATCTTGCTCAGGTGGCAGGTCCAGCGGAAAGTGATCTGC
ATCCCCAAAAGTATCACTCCTTCTCGAATCCTTCAGAACATCAAGGTGTTTGACTTCACC
TTTAGCCCAGAAGAGATGAAGCAGCTAAATGCCCTGAACAAAAATTGGAGATATATTGTG
CCTATGCTTACGGTGGATGGGAAGAGAGTCCCAAGGGATGCAGGGCATCCTCTGTACCCC
TTTAATGACCCGTACTGA
Enzyme 3 GenBank Gene ID J04794 Link Image
Enzyme 3 GeneCard ID AKR1A1 Link Image
Enzyme 3 GenAtlas ID AKR1A1 Link Image
Enzyme 3 HGNC ID HGNC:380 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1p33-p32
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Bohren KM, Bullock B, Wermuth B, Gabbay KH: The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J Biol Chem. 1989 Jun 5;264(16):9547-51. [PubMed Link Image]
  2. Fujii J, Hamaoka R, Matsumoto A, Fujii T, Yamaguchi Y, Egashira M, Miyoshi O, Niikawa N, Taniguchi N: The structural organization of the human aldehyde reductase gene, AKR1A1, and mapping to chromosome 1p33-->p32. Cytogenet Cell Genet. 1999;84(3-4):230-2. [PubMed Link Image]
  3. Barski OA, Gabbay KH, Bohren KM: Characterization of the human aldehyde reductase gene and promoter. Genomics. 1999 Sep 1;60(2):188-98. [PubMed Link Image]
  4. 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]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. 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]
  7. Wermuth B, Omar A, Forster A, di Francesco C, Wolf M, von Wartburg JP, Bullock B, Gabbay KH: Primary structure of aldehyde reductase from human liver. Prog Clin Biol Res. 1987;232:297-307. [PubMed Link Image]
  8. Barski OA, Gabbay KH, Grimshaw CE, Bohren KM: Mechanism of human aldehyde reductase: characterization of the active site pocket. Biochemistry. 1995 Sep 5;34(35):11264-75. [PubMed Link Image]
  9. O'connor T, Ireland LS, Harrison DJ, Hayes JD: Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members. Biochem J. 1999 Oct 15;343 Pt 2:487-504. [PubMed Link Image]
  10. Palackal NT, Burczynski ME, Harvey RG, Penning TM: Metabolic activation of polycyclic aromatic hydrocarbon trans-dihydrodiols by ubiquitously expressed aldehyde reductase (AKR1A1). Chem Biol Interact. 2001 Jan 30;130-132(1-3):815-24. [PubMed Link Image]
  11. Bains OS, Takahashi RH, Pfeifer TA, Grigliatti TA, Reid RE, Riggs KW: Two allelic variants of aldo-keto reductase 1A1 exhibit reduced in vitro metabolism of daunorubicin. Drug Metab Dispos. 2008 May;36(5):904-10. Epub 2008 Feb 14. [PubMed Link Image]
  12. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  13. El-Kabbani O, Green NC, Lin G, Carson M, Narayana SV, Moore KM, Flynn TG, DeLucas LJ: Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications. Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):859-68. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available