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Human Metabolome Database Version 2.5

 

Showing metabocard for 2-Amino-3-carboxymuconic acid semialdehyde (HMDB01330)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:44
Accession Number HMDB01330
Secondary Accession Numbers Not Available
Common Name 2-Amino-3-carboxymuconic acid semialdehyde
Description 2-amino-3-carboxymuconic acid semialdehyde is an intermediate metabolite of the tryptophan-niacin catabolic pathway. Current interest in the degradation of tryptophan is mostly due to the role of quinolinate and other metabolites in several neuropathological conditions. Quinolinate is a neurotoxin formed nonenzymatically from 2-amino-3-carboxymuconic semialdehyde in mammalian tissues. 2-Amino-3-carboxymuconic semialdehyde is enzymatically converted to 2-aminomuconate via 2-aminomuconic semialdehyde. (PMID: 10510494, 16267312, 14275129)
Synonyms
  1. ACS
  2. 2-amino-3-carboxymuconate semialdehyde
  3. 2-amino-3-carboxymuconate-6-semialdehyde
  4. 2-Amino-3-(3-oxoprop-1-enyl)-but-2-enedioate
  5. Amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
  6. 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
  7. 2-Amino-3-(3-oxoprop-1-enyl)-but-2-enedioic acid
  8. Amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioic acid
  9. 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioic acid
Chemical IUPAC Name 2-amino-3-(3-oxoprop-1-enyl)but-2-enedioic acid
Chemical Formula C7H7NO5
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • aldehyde
  • enamine
  • carboxylic acid
  • alkene
Biofunction
  • Component of Tryptophan metabolism
Application
Source
  • Endogenous
Average Molecular Weight 185.134
Monoisotopic Molecular Weight 185.032425
Isomeric SMILES NC(C(O)=O)=C(C=C/C=O)C(O)=O
Canonical SMILES NC(C(O)=O)=C(C=CC=O)C(O)=O
KEGG Compound ID C04409 Link Image
BioCyc ID 2-AMINO-3-CARBOXYMUCONATE_SEMIAL Link Image
BiGG ID 1445617 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01330 Link Image
Metagene Link HMDB01330 Link Image
METLIN ID 6165 Link Image
PubChem Compound 23 Link Image
PubChem Substance 1934 Link Image
ChEBI ID 29044 Link Image
CAS Registry Number 16597-58-3
InChI Identifier InChI=1/C7H7NO5/c8-5(7(12)13)4(6(10)11)2-1-3-9/h1-3H,8H2,(H,10,11)(H,12,13)/b2-1-,5-4-
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.64 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.05 [Predicted by ALOGPS]; -3.2 [Predicted by PubChem via XLOGP] 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
  • Cytoplasm
Biofluid Location Not Available
Tissue Location
Tissue References
Brain
Kidney
Liver
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Tryptophan Metabolism SMP00063 Link Image map00380 Link Image
General References
  1. Ftukijwatari T, Murakami M, Ohta M, Kimura N, Jin-No Y, Sasaki R, Shibata K: Changes in the urinary excretion of the metabolites of the tryptophan-niacin pathway during pregnancy in Japanese women and rats. J Nutr Sci Vitaminol (Tokyo). 2004 Dec;50(6):392-8. [PubMed Link Image]
Metabolic Enzymes
  1. 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
  2. 3-hydroxyanthranilate 3,4-dioxygenase
Enzyme 1 [top]
Enzyme 1 ID 5493
Enzyme 1 Name 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
Enzyme 1 Synonyms
  1. Picolinate carboxylase
Enzyme 1 Gene Name ACMSD
Enzyme 1 Protein Sequence >2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
MKIDIHSHILPKEWPDLKKRFGYGGWVQLQHHSKGEAKLLKDGKVFRVVRENCWDPEVRI
REMDQKGVTVQALSTVPVMFSYWAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQ
APELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMQM
DGRMAKYWLPWLVGMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGF
SMRPDLCAQDNPMNPKKYLGSFYTDALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGELE
PGKLIESMEEFDEETKNKLKAGNALAFLGLERKQFE
Enzyme 1 Number of Residues 336
Enzyme 1 Molecular Weight 38035.0
Enzyme 1 Theoretical pI 6.99
Enzyme 1 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 1 General Function Involved in catalytic activity
Enzyme 1 Specific Function Converts alpha-amino-beta-carboxymuconate-epsilon- semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal cells which is implicated in the pathogenesis of various neurodegenerative disorders. In the presence of ACMSD, ACMS is converted to AMS, a benign catabolite. ACMSD ultimately controls the metabolic fate of tryptophan catabolism along the kynurenine pathway
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate = 2-aminomuconate semialdehyde + CO2 [RN:R04323]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 19911227 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q8TDX5 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ACMSD_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1011 bp
ATGAAAATTGACATCCATAGTCATATTCTACCAAAAGAATGGCCAGATCTAAAAAAGAGG
TTTGGCTACGGAGGCTGGGTGCAGCTCCAACACCACAGCAAGGGAGAAGCAAAGTTGTTG
AAAGATGGGAAAGTCTTCAGAGTGGTGCGAGAGAATTGCTGGGATCCAGAAGTTCGTATT
AGAGAAATGGACCAAAAAGGAGTAACAGTGCAAGCCCTTTCCACAGTTCCTGTCATGTTT
AGCTACTGGGCCAAACCTGAGGACACTTTAAACCTGTGCCAGCTTTTAAACAACGACCTT
GCCAGCACCGTTGTGAGCTACCCCAGGAGGTTCGTGGGTCTGGGGACGTTGCCCATGCAG
GCCCCTGAGCTGGCGGTCAAGGAGATGGAGCGCTGTGTGAAAGAGCTGGGCTTTCCCGGG
GTCCAAATTGGCACCCACGTCAACGAGTGGGACCTGAACGCGCAGGAGCTCTTTCCTGTC
TATGCGGCAGCCGAAAGGCTGAAGTGTTCCCTGTTCGTGCATCCCTGGGACATGCAGATG
GATGGACGAATGGCCAAATACTGGCTCCCTTGGCTTGTAGGAATGCCAGCAGAGACCACC
ATAGCCATTTGCTCCATGATCATGGGTGGAGTATTTGAGAAGTTTCCCAAACTGAAAGTG
TGTTTCGCACATGGTGGTGGTGCCTTCCCCTTCACAGTGGGAAGAATCTCCCATGGATTC
AGCATGCGCCCAGATCTGTGTGCCCAGGACAACCCCATGAACCCGAAGAAATACCTTGGT
TCCTTTTACACAGATGCTTTGGTTCATGATCCTCTGTCCCTCAAGCTGTTAACAGATGTC
ATAGGAAAGGATAAAGTCATTTTGGGAACCGATTACCCCTTTCCACTAGGTGAGCTGGAA
CCTGGGAAACTAATAGAGTCCATGGAAGAATTTGATGAAGAAACAAAGAATAAACTCAAA
GCCGGCAATGCCCTGGCATTTTTGGGTCTTGAGAGAAAACAATTTGAATGA
Enzyme 1 GenBank Gene ID AB071418 Link Image
Enzyme 1 GeneCard ID ACMSD Link Image
Enzyme 1 GenAtlas ID ACMSD Link Image
Enzyme 1 HGNC ID HGNC:19288 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2q21.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Fukuoka S, Ishiguro K, Yanagihara K, Tanabe A, Egashira Y, Sanada H, Shibata K: Identification and expression of a cDNA encoding human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD). A key enzyme for the tryptophan-niacine pathway and "quinolinate hypothesis". J Biol Chem. 2002 Sep 20;277(38):35162-7. Epub 2002 Jul 24. [PubMed Link Image]
  2. 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]
  3. Garavaglia S, Perozzi S, Galeazzi L, Raffaelli N, Rizzi M: The crystal structure of human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase in complex with 1,3-dihydroxyacetonephosphate suggests a regulatory link between NAD synthesis and glycolysis. FEBS J. 2009 Nov;276(22):6615-23. Epub 2009 Oct 16. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6424
Enzyme 2 Name 3-hydroxyanthranilate 3,4-dioxygenase
Enzyme 2 Synonyms
  1. 3-hydroxyanthranilate oxygenase
  2. 3-HAO
  3. 3-hydroxyanthranilic acid dioxygenase
  4. HAD
Enzyme 2 Gene Name HAAO
Enzyme 2 Protein Sequence >3-hydroxyanthranilate 3,4-dioxygenase
MERRLGVRAWVKENRGSFQPPVCNKLMHQEQLKVMFIGGPNTRKDYHIEEGEEVFYQLEG
DMVLRVLEQGKHRDVVIRQGEIFLLPARVPHSPQRFANTVGLVVERRRLETELDGLRYYV
GDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGKPIPDQLLKEPPFPLSTRSIMEP
MSLDAWLDSHHRELQAGTPLSLFGDTYETQVIAYGQGSSEGLRQNVDVWLWQLEGSSVVT
MGGRRLSLAPDDSLLVLAGTSYAWERTQGSVALSVTQDPACKKPLG
Enzyme 2 Number of Residues 286
Enzyme 2 Molecular Weight 32555.9
Enzyme 2 Theoretical pI 5.69
Enzyme 2 GO Classification
Function
  • 3-hydroxyanthranilate 3,4-dioxygenase activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 2 General Function Involved in 3-hydroxyanthranilate 3,4-dioxygenase activity
Enzyme 2 Specific Function Catalyzes the oxidative ring opening of 3- hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde [RN:R02665]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 62822152 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P46952 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name 3HAO_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >861 bp
ATGGAGCGCCGCCTGGGAGTGAGGGCCTGGGTGAAGGAGAACCGGGGCTCCTTCCAGCCC
CCGGTCTGCAACAAGCTCATGCACCAGGAGCAGCTCAAAGTCATGTTCATCGGAGGCCCC
AACACCAGGAAGGACTATCACATCGAAGAGGGTGAAGAGGTATTTTACCAGCTGGAGGGA
GACATGGTTCTCCGAGTCCTGGAGCAAGGGAAACACCGGGATGTGGTCATTCGGCAGGGA
GAGATATTCCTCCTGCCTGCCAGGGTGCCCCACTCACCACAGAGGTTTGCCAACACCGTG
GGGCTGGTGGTTGAGCGAAGGCGGCTGGAGACCGAGCTAGATGGGCTCAGGTACTATGTG
GGCGACACCATGGACGTTCTGTTTGAGAAGTGGTTCTACTGCAAGGACCTCGGCACGCAG
TTGGCCCCCATCATCCAGGAGTTCTTCAGCTCTGAGCAGTACAGAACAGGAAAGCCCATC
CCTGACCAGCTGCTCAAGGAGCCACCATTCCCTCTGAGCACACGATCCATCATGGAGCCC
ATGTCCCTGGATGCCTGGCTGGACAGCCACCACAGGGAGCTGCAGGCAGGCACACCACTC
AGCCTGTTTGGGGACACCTATGAGACCCAGGTGATCGCCTATGGGCAAGGCAGCAGCGAA
GGCCTGAGACAGAATGTGGACGTGTGGCTGTGGCAGCTGGAGGGCTCCTCGGTGGTGACA
ATGGGGGGACGGCGCCTGAGCCTGGCCCCTGATGACAGCCTCCTGGTGCTAGCTGGGACC
TCGTATGCCTGGGAGCGAACACAAGGCTCTGTGGCCCTGTCTGTGACCCAGGACCCTGCC
TGCAAGAAGCCCCTGGGGTGA
Enzyme 2 GenBank Gene ID AC098824 Link Image
Enzyme 2 GeneCard ID HAAO Link Image
Enzyme 2 GenAtlas ID HAAO Link Image
Enzyme 2 HGNC ID HGNC:4796 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2p21
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Malherbe P, Kohler C, Da Prada M, Lang G, Kiefer V, Schwarcz R, Lahm HW, Cesura AM: Molecular cloning and functional expression of human 3-hydroxyanthranilic-acid dioxygenase. J Biol Chem. 1994 May 13;269(19):13792-7. [PubMed Link Image]
  2. 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]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [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]
Enzyme 2 Metabolite References Not Available