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Human Metabolome Database Version 2.5

 

Showing metabocard for Oxoadipic acid (HMDB00225)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-26 21:15:14
Accession Number HMDB00225
Secondary Accession Numbers Not Available
Common Name Oxoadipic acid
Description 2-Oxoadipic acid is produced from lysine in the cytosol of cells via the saccharopine and the pipecolic acid pathways. Catabolites of hydroxylysine and tryptophan enter these pathways as 2-aminoadipic- -semialdehyde and 2-oxoadipate, respectively. In the matrix of mitochondria, 2-oxoadipate is decarboxylated to glutaryl-CoA by the 2-oxoadipate dehydrogenase complex and then converted to acetyl-CoA. 2-Oxoadipic aciduria is an in-born error of metabolism of lysine, tryptophan, and hydroxylysine, in which abnormal quantities of 2-aminoadipic acid are found in body fluids along with 2-oxoadipic acid. Patients with 2-Oxoadipic acidemias are mentally retarded with hypotonia or seizures. 2-Oxoadipic Aciduria can occur in patients with Kearns-Sayre Syndrome, a progressive disorder with onset prior to 20 years of age in which multiple organ systems are affected, including progressive external ophthalmoplegia, retinopathy, and the age of onset, and these are associated classically with abnormalities in cardiac conduction, cerebellar signs, and elevated cerebrospinal fluid protein. (PMID: 10655159, 16183823, 11083877)
Synonyms
  1. alpha-ketoadipic acid
  2. alpha-Oxoadipic acid
  3. alpha-Oxoadipate
  4. alpha-Ketoadipate
  5. a-Oxoadipic acid
  6. a-Oxoadipate
  7. a-Ketoadipic acid
  8. a-Ketoadipate
  9. Oxoadipate
  10. 2-oxohexanedionic acid
  11. 2-oxoadipate
  12. 2-ketoadipate
  13. 2-keto-adipate
  14. 2-Oxohexanedioic acid
  15. 2-Oxohexanedioate
  16. 2-Oxoadipic acid
  17. 2-Oxo-hexanedioic acid
  18. 2-Ketoadipic acid
  19. 2-Oxo-hexanedioate
Chemical IUPAC Name 2-oxohexanedioic acid
Chemical Formula C6H8O5
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Dicarboxylic Acids
  • Keto-Acids
Sub Class
  • Short chain dicarboxylic acids
Family
  • Mammalian Metabolite
Species
  • ketone
  • carboxylic acid
Biofunction
  • Component of Lysine biosynthesis
Application
Source
  • Endogenous
Average Molecular Weight 160.125
Monoisotopic Molecular Weight 160.037170
Isomeric SMILES OC(=O)CCCC(=O)C(O)=O
Canonical SMILES OC(=O)CCCC(=O)C(O)=O
KEGG Compound ID C00322 Link Image
BioCyc ID 2K-ADIPATE Link Image
BiGG ID 1485244 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB00225 Link Image
Metagene Link HMDB00225 Link Image
METLIN ID 5234 Link Image
PubChem Compound 71 Link Image
PubChem Substance 10329255 Link Image
ChEBI ID 15753 Link Image
CAS Registry Number 3184-35-8
InChI Identifier InChI=1/C6H8O5/c7-4(6(10)11)2-1-3-5(8)9/h1-3H2,(H,8,9)(H,10,11)
Synthesis Reference Nelson, Randall B.; Gribble, Gordon W. Preparation of a-ketoadipic acid. Organic Preparations and Procedures International (1973), 5(2), 55-8.
Melting Point (Experimental) 127
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 23.4 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.37 [Predicted by ALOGPS]; -0.7 [Predicted by PubChem via XLOGP] 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 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 (Predicted from LogP)
  • mitochondria
Biofluid Location
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Urine
Value 0.17 (0.02-0.57) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Lee SH, Kim SO, Chung BC: Gas chromatographic-mass spectrometric determination of urinary oxoacids using O-(2,3,4,5,6-pentafluorobenzyl)oxime-trimethylsilyl ester derivatization and cation-exchange chromatography. J Chromatogr B Biomed Sci Appl. 1998 Nov 20;719(1-2):1-7. [PubMed Link Image]
Biofluid Urine
Value 0.21 (0.04-0.81) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Lee SH, Kim SO, Chung BC: Gas chromatographic-mass spectrometric determination of urinary oxoacids using O-(2,3,4,5,6-pentafluorobenzyl)oxime-trimethylsilyl ester derivatization and cation-exchange chromatography. J Chromatogr B Biomed Sci Appl. 1998 Nov 20;719(1-2):1-7. [PubMed Link Image]
Biofluid Urine
Value 1.3 (1.0-1.5) umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Children aged 2-6 years
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 1.2 (1.2-1.2) umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Children aged 6-10 years
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Urine
Value 1.0 (0.00-2.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition 2-ketoadipic acidemia
Comments Not Available
References
Biofluid Urine
Value 120.0 (20.0-220.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition 2-ketoadipic acidemia
Comments Not Available
References
Associated Disorders
Condition References
2-ketoadipic acidemia
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Lysine Degradation SMP00037 Link Image map00310 Link Image
General References
  1. Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
  2. Lee SH, Kim SO, Chung BC: Gas chromatographic-mass spectrometric determination of urinary oxoacids using O-(2,3,4,5,6-pentafluorobenzyl)oxime-trimethylsilyl ester derivatization and cation-exchange chromatography. J Chromatogr B Biomed Sci Appl. 1998 Nov 20;719(1-2):1-7. [PubMed Link Image]
Metabolic Enzymes
  1. Dihydrolipoyl dehydrogenase, mitochondrial
  2. 2-oxoglutarate dehydrogenase, mitochondrial
  3. Aminoadipate aminotransferase, isoform CRA_b
  4. 2-oxoglutarate dehydrogenase-like, mitochondrial
  5. Putative uncharacterized protein
Enzyme 1 [top]
Enzyme 1 ID 5283
Enzyme 1 Name Dihydrolipoyl dehydrogenase, mitochondrial
Enzyme 1 Synonyms
  1. Dihydrolipoamide dehydrogenase
  2. Glycine cleavage system L protein
Enzyme 1 Gene Name DLD
Enzyme 1 Protein Sequence >Dihydrolipoyl dehydrogenase, mitochondrial
MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKA
AQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNL
DKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNIL
IATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVT
AVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGK
AEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGP
MLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGK
FPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDI
ARVCHAHPTLSEAFREANLAASFGKSINF
Enzyme 1 Number of Residues 509
Enzyme 1 Molecular Weight 54176.9
Enzyme 1 Theoretical pI 7.95
Enzyme 1 GO Classification
Function
  • FAD or FADH2 binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • dihydrolipoyl dehydrogenase activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on a sulfur group of donors, NAD or NADP as acceptor
  • purine nucleoside binding
Process
  • cell redox homeostasis
  • cellular homeostasis
  • cellular process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 1 General Function Involved in oxidoreductase activity
Enzyme 1 Specific Function Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction
Enzyme 1 Pathways
Enzyme 1 Reactions
  • protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+ [RN:R08550]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 91199540 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P09622 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name DLDH_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1530 bp
ATGCAGAGCTGGAGTCGTGTGTACTGCTCCTTGGCCAAGAGAGGCCATTTCAATCGAATA
TCTCATGGCCTACAGGGACTTTCTGCAGTGCCTCTGAGAACTTACGCAGATCAGCCGATT
GATGCTGATGTAACAGTTATAGGTTCTGGTCCTGGAGGATATGTTGCTGCTATTAAAGCT
GCCCAGTTAGGCTTCAAGACAGTCTGCATTGAGAAAAATGAAACACTTGGTGGAACATGC
TTGAATGTTGGTTGTATTCCTTCTAAGGCTTTATTGAACAACTCTCATTATTACCATATG
GCCCATGGAAAAGATTTTGCATCTAGAGGAATTGAAATGTCCGAAGTTCGCTTGAATTTA
GACAAGATGATGGAGCAGAAGAGTACTGCAGTAAAAGCTTTAACAGGTGGAATTGCCCAC
TTATTCAAACAGAATAAGGTTGTTCATGTCAATGGATATGGAAAGATAACTGGCAAAAAT
CAAGTCACTGCTACGAAAGCTGATGGCGGCACTCAGGTTATTGATACAAAGAACATTCTT
ATAGCCACGGGTTCAGAAGTTACTCCTTTTCCTGGAATCACGATAGATGAAGATACAATA
GTGTCATCTACAGGTGCTTTATCTTTAAAAAAAGTTCCAGAAAAGATGGTTGTTATTGGT
GCAGGAGTAATAGGTGTAGAATTGGGTTCAGTTTGGCAAAGACTTGGTGCAGATGTGACA
GCAGTTGAATTTTTAGGTCATGTAGGTGGAGTTGGAATTGATATGGAGATATCTAAAAAC
TTTCAACGCATCCTTCAAAAACAGGGGTTTAAATTTAAATTGAATACAAAGGTTACTGGT
GCTACCAAGAAGTCAGATGGAAAAATTGATGTTTCTATTGAAGCTGCTTCTGGTGGTAAA
GCTGAAGTTATCACTTGTGATGTACTCTTGGTTTGCATTGGCCGACGACCCTTTACTAAG
AATTTGGGACTAGAAGAGCTGGGAATTGAACTAGATCCCAGAGGTAGAATTCCAGTCAAT
ACCAGATTTCAAACTAAAATTCCAAATATCTATGCCATTGGTGATGTAGTTGCTGGTCCA
ATGCTGGCTCACAAAGCAGAGGATGAAGGCATTATCTGTGTTGAAGGAATGGCTGGTGGT
GCTGTGCACATTGACTACAATTGTGTGCCATCAGTGATTTACACACACCCTGAAGTTGCT
TGGGTTGGCAAATCAGAAGAGCAGTTGAAAGAAGAGGGTATTGAGTACAAAGTTGGGAAA
TTCCCATTTGCTGCTAACAGCAGAGCTAAGACAAATGCTGACACAGATGGCATGGTGAAG
ATCCTTGGGCAGAAATCGACAGACAGAGTACTGGGAGCACATATTCTTGGACCAGGTGCT
GGAGAAATGGTAAATGAAGCTGCTCTTGCTTTGGAATATGGAGCATCCTGTGAAGATATA
GCTAGAGTCTGTCATGCACATCCGACCTTATCAGAAGCTTTTAGAGAAGCAAATCTTGCT
GCGTCATTTGGCAAATCAATCAACTTTTGA
Enzyme 1 GenBank Gene ID NM_000108.3 Link Image
Enzyme 1 GeneCard ID DLD Link Image
Enzyme 1 GenAtlas ID DLD Link Image
Enzyme 1 HGNC ID HGNC:2898 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7q31-q32
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Otulakowski G, Robinson BH: Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases. J Biol Chem. 1987 Dec 25;262(36):17313-8. [PubMed Link Image]
  2. Pons G, Raefsky-Estrin C, Carothers DJ, Pepin RA, Javed AA, Jesse BW, Ganapathi MK, Samols D, Patel MS: Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component human alpha-ketoacid dehydrogenase complexes. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1422-6. [PubMed Link Image]
  3. Feigenbaum AS, Robinson BH: The structure of the human dihydrolipoamide dehydrogenase gene (DLD) and its upstream elements. Genomics. 1993 Aug;17(2):376-81. [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. 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]
  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. Johanning GL, Morris JI, Madhusudhan KT, Samols D, Patel MS: Characterization of the transcriptional regulatory region of the human dihydrolipoamide dehydrogenase gene. Proc Natl Acad Sci U S A. 1992 Nov 15;89(22):10964-8. [PubMed Link Image]
  8. 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]
  9. Brautigam CA, Chuang JL, Tomchick DR, Machius M, Chuang DT: Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations. J Mol Biol. 2005 Jul 15;350(3):543-52. [PubMed Link Image]
  10. Ciszak EM, Makal A, Hong YS, Vettaikkorumakankauv AK, Korotchkina LG, Patel MS: How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex. J Biol Chem. 2006 Jan 6;281(1):648-55. Epub 2005 Nov 1. [PubMed Link Image]
  11. Brautigam CA, Wynn RM, Chuang JL, Machius M, Tomchick DR, Chuang DT: Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex. Structure. 2006 Mar;14(3):611-21. Epub 2006 Jan 26. [PubMed Link Image]
  12. Liu TC, Kim H, Arizmendi C, Kitano A, Patel MS: Identification of two missense mutations in a dihydrolipoamide dehydrogenase-deficient patient. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5186-90. [PubMed Link Image]
  13. Hong YS, Kerr DS, Craigen WJ, Tan J, Pan Y, Lusk M, Patel MS: Identification of two mutations in a compound heterozygous child with dihydrolipoamide dehydrogenase deficiency. Hum Mol Genet. 1996 Dec;5(12):1925-30. [PubMed Link Image]
  14. Shaag A, Saada A, Berger I, Mandel H, Joseph A, Feigenbaum A, Elpeleg ON: Molecular basis of lipoamide dehydrogenase deficiency in Ashkenazi Jews. Am J Med Genet. 1999 Jan 15;82(2):177-82. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5677
Enzyme 2 Name 2-oxoglutarate dehydrogenase, mitochondrial
Enzyme 2 Synonyms
  1. 2-oxoglutarate dehydrogenase complex component E1
  2. OGDC-E1
  3. Alpha-ketoglutarate dehydrogenase
Enzyme 2 Gene Name OGDH
Enzyme 2 Protein Sequence >2-oxoglutarate dehydrogenase, mitochondrial
MFHLRTCAAKLRPLTASQTVKTFSQNRPAAARTFQQIRCYSAPVAAEPFLSGTSSNYVEE
MYCAWLENPKSVHKSWDIFFRNTNAGAPPGTAYQSPLPLSRGSLAAVAHAQSLVEAQPNV
DKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGILDADLDSSVPADIISSTDKLGFYGLDES
DLDKVFHLPTTTFIGGQESALPLREIIRRLEMAYCQHIGVEFMFINDLEQCQWIRQKFET
PGIMQFTNEEKRTLLARLVRSTRFEEFLQRKWSSEKRFGLEGCEVLIPALKTIIDKSSEN
GVDYVIMGMPHRGRLNVLANVIRKELEQIFCQFDSKLEAADEGSGDVKYHLGMYHRRINR
VTDRNITLSLVANPSHLEAADPVVMGKTKAEQFYCGDTEGKKVMSILLHGDAAFAGQGIV
YETFHLSDLPSYTTHGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNSDDP
EAVMYVCKVAAEWRSTFHKDVVVDLVCYRRNGHNEMDEPMFTQPLMYKQIRKQKPVLQKY
AELLVSQGVVNQPEYEEEISKYDKICEEAFARSKDEKILHIKHWLDSPWPGFFTLDGQPR
SMSCPSTGLTEDILTHIGNVASSVPVENFTIHGGLSRILKTRGEMVKNRTVDWALAEYMA
FGSLLKEGIHIRLSGQDVERGTFSHRHHVLHDQNVDKRTCIPMNHLWPNQAPYTVCNSSL
SEYGVLGFELGFAMASPNALVLWEAQFGDFHNTAQCIIDQFICPGQAKWVRQNGIVLLLP
HGMEGMGPEHSSARPERFLQMCNDDPDVLPDLKEANFDINQLYDCNWVVVNCSTPGNFFH
VLRRQILLPFRKPLIIFTPKSLLRHPEARSSFDEMLPGTHFQRVIPEDGPAAQNPENVKR
LLFCTGKVYYDLTRERKARDMVGQVAITRIEQLSPFPFDLLLKEVQKYPNAELAWCQEEH
KNQGYYDYVKPRLRTTISRAKPVWYAGRDPAAAPATGNKKTHLTELQRLLDTAFDLDVFK
NFS
Enzyme 2 Number of Residues 1023
Enzyme 2 Molecular Weight 115934.4
Enzyme 2 Theoretical pI 6.86
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
  • oxoglutarate dehydrogenase (succinyl-transferring) activity
  • thiamin pyrophosphate binding
  • vitamin binding
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 2 General Function Involved in oxoglutarate dehydrogenase (succinyl-transferring) activity
Enzyme 2 Specific Function The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components:2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3)
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2 [RN:R01700]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 37674435 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q02218 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ODO1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >3072 bp
ATGTTTCATTTAAGGACTTGTGCTGCTAAGTTGAGGCCATTGACGGCTTCCCAGACTGTT
AAGACATTTTCACAAAACAGACCAGCAGCAGCTAGGACATTTCAACAGATTCGGTGCTAT
TCTGCACCTGTTGCTGCTGAGCCCTTTCTCAGTGGGACTAGTTCGAACTATGTGGAGGAG
ATGTACTGTGCTTGGCTGGAAAACCCCAAAAGTGTACATAAGTCATGGGACATTTTTTTT
CGCAACACGAATGCCGGAGCCCCACCGGGCACTGCCTACCAGAGTCCCCTTCCCCTGAGC
CGAGGCTCCCTGGCTGCTGTGGCCCATGCACAGTCCCTGGTAGAAGCACAGCCCAACGTG
GACAAGCTCGTGGAGGACCACCTGGCAGTGCAGTCGCTCATCAGGGCATATCAGATACGA
GGGCACCATGTAGCACAGCTGGACCCCCTGGGGATTTTGGATGCTGATCTGGACTCCTCC
GTGCCCGCTGACATTATCTCATCCACAGACAAACTTGGGTTCTATGGCCTGGATGAGTCT
GACCTCGACAAGGTCTTCCACTTGCCCACCACCACTTTCATCGGGGGACAGGAATCAGCA
CTTCCTCTGCGGGAGATCATCCGTCGGCTGGAGATGGCCTACTGCCAGCATATTGGGGTG
GAGTTCATGTTCATCAATGACCTGGAGCAGTGCCAGTGGATCCGGCAGAAGTTTGAGACC
CCTGGGATCATGCAGTTCACAAATGAGGAGAAACGGACCCTGCTGGCCAGGCTTGTGCGG
TCCACCAGGTTTGAGGAGTTCCTACAGCGGAAGTGGTCCTCTGAGAAGCGCTTTGGTCTA
GAAGGCTGCGAGGTACTGATCCCTGCCCTCAAGACCATCATTGACAAGTCTAGTGAGAAT
GGCGTGGACTACGTGATCATGGGCATGCCACACAGAGGGCGGCTGAACGTGCTTGCAAAT
GTCATCAGGAAGGAGCTGGAACAGATCTTCTGTCAATTCGATTCAAAGCTGGAGGCAGCT
GATGAGGGCTCCGGAGATGTGAAGTACCACCTGGGCATGTATCACCGCAGGATCAATCGT
GTCACCGACAGGAACATTACCTTGTCCTTGGTGGCCAACCCTTCCCACCTTGAGGCCGCT
GACCCCGTGGTGATGGGCAAGACCAAAGCCGAACAGTTTTACTGTGGCGACACTGAAGGG
AAAAAGGTCATGTCCATCCTGTTGCATGGGGATGCTGCATTTGCTGGCCAGGGCATTGTG
TACGAGACCTTCCACCTCAGCGACCTGCCATCCTACACAACTCATGGCACCGTGCACGTG
GTCGTCAACAACCAGATCGGCTTCACCACCGACCCTCGGATGGCCCGCTCCTCCCCCTAC
CCCACTGACGTGGCCCGAGTGGTGAATGCCCCCATTTTCCACGTGAACTCAGATGACCCC
GAGGCTGTCATGTACGTGTGCAAAGTGGCGGCCGAGTGGAGGAGCACCTTCCACAAGGAC
GTGGTTGTCGATTTGGTGTGTTACCGGCGCAACGGCCACAACGAGATGGATGAGCCCATG
TTCACGCAGCCGCTCATGTACAAGCAGATCCGCAAGCAGAAGCCTGTGTTACAGAAGTAC
GCTGAGCTGCTGGTGTCGCAGGGTGTGGTCAACCAGCCTGAGTATGAGGAGGAAATTTCC
AAGTATGATAAGATCTGTGAGGAAGCTTTTGCCAGATCTAAAGATGAGAAGATCTTGCAC
ATTAAGCACTGGCTGGACTCTCCCTGGCCTGGCTTCTTCACCCTGGACGGGCAGCCCAGG
AGCATGTCCTGCCCCTCCACGGGTCTGACGGAGGATATTCTGACACACATCGGGAATGTG
GCTAGTTCTGTGCCTGTGGAAAACTTTACTATTCATGGAGGGCTGAGCCGGATCTTGAAG
ACTCGTGGGGAAATGGTGAAGAACCGGACTGTGGACTGGGCTCTAGCGGAGTACATGGCG
TTTGGCTCGCTCCTGAAGGAGGGCATCCACATTCGGCTGAGCGGCCAGGACGTGGAGCGG
GGCACATTCAGCCACCGCCACCATGTGCTCCATGACCAGAATGTGGACAAGAGAACCTGC
ATCCCCATGAACCATCTCTGGCCCAATCAGGCCCCCTATACTGTGTGCAACAGCTCACTG
TCTGAGTACGGCGTGCTGGGCTTTGAGCTGGGCTTCGCCATGGCCAGTCCTAATGCCCTG
GTCCTCTGGGAAGCCCAATTTGGTGACTTCCACAACACGGCCCAGTGTATCATCGACCAG
TTCATCTGCCCGGGACAAGCCAAGTGGGTGCGGCAGAATGGCATCGTGTTGCTGCTGCCC
CATGGCATGGAGGGCATGGGTCCAGAACATTCCTCCGCCCGCCCAGAGCGGTTCTTGCAG
ATGTGCAACGATGACCCAGATGTCCTGCCAGACCTTAAAGAAGCCAACTTCGACATCAAT
CAGCTATATGACTGCAATTGGGTTGTTGTCAACTGCTCCACTCCTGGCAACTTCTTCCAC
GTGCTACGACGCCAGATCCTGCTGCCATTCCGGAAGCCGTTAATTATCTTCACCCCCAAA
TCCCTGTTGCGCCACCCCGAGGCCAGATCCAGCTTTGATGAGATGCTTCCAGGAACCCAC
TTCCAGCGGGTGATCCCAGAAGATGGCCCTGCAGCTCAGAACCCAGAAAATGTCAAAAGG
CTTCTCTTCTGCACCGGCAAAGTGTATTATGACCTCACCCGGGAGCGCAAAGCACGCGAC
ATGGTGGGGCAGGTGGCCATCACAAGGATTGAGCAGCTGTCGCCATTCCCCTTTGACCTC
CTGCTGAAGGAGGTGCAGAAGTACCCCAATGCTGAGCTGGCCTGGTGCCAGGAGGAGCAC
AAGAACCAAGGCTACTATGACTACGTGAAGCCAAGACTTCGGACCACCATCAGCCGCGCC
AAGCCCGTCTGGTATGCCGGCCGGGACCCAGCGGCTGCTCCAGCCACCGGCAACAAGAAG
ACCCACCTGACGGAGCTGCAGCGCCTCCTGGACACGGCCTTCGACCTGGACGTCTTCAAG
AACTTCTCGTAG
Enzyme 2 GenBank Gene ID AC004859 Link Image
Enzyme 2 GeneCard ID OGDH Link Image
Enzyme 2 GenAtlas ID OGDH Link Image
Enzyme 2 HGNC ID HGNC:8124 Link Image
Enzyme 2 Chromosome Location 7
Enzyme 2 Locus 7p14-p13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Koike K, Urata Y, Goto S: Cloning and nucleotide sequence of the cDNA encoding human 2-oxoglutarate dehydrogenase (lipoamide). Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1963-7. [PubMed Link Image]
  2. Koike K: The gene encoding human 2-oxoglutarate dehydrogenase: structural organization and mapping to chromosome 7p13-p14. Gene. 1995 Jul 4;159(2):261-6. [PubMed Link Image]
  3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [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. Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D: Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry. Proteomics. 2007 Mar;7(6):868-74. [PubMed Link Image]
  6. 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]
  7. Jones LL, Colf LA, Bankovich AJ, Stone JD, Gao YG, Chan CM, Huang RH, Garcia KC, Kranz DM: Different thermodynamic binding mechanisms and peptide fine specificities associated with a panel of structurally similar high-affinity T cell receptors. Biochemistry. 2008 Nov 25;47(47):12398-408. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 8585
Enzyme 3 Name Aminoadipate aminotransferase, isoform CRA_b
Enzyme 3 Synonyms
  1. SubName: Putative uncharacterized protein AADAT
  2. SubName: cDNA, FLJ95590, Homo sapiens L-kynurenine/alpha-aminoadipate aminotransferase (KATII), mRNA
Enzyme 3 Gene Name AADAT
Enzyme 3 Protein Sequence >Aminoadipate aminotransferase, isoform CRA_b
MNYARFITAASAARNPSPIRTMTDILSRGPKSMISLAGGLPNPNMFPFKTAVITVENGKT
IQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDLCVTSGSQQG
LCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVASDESGIVPDSLRDILSRWKP
EDAKNPQKNTPKFLYTVPNGNNPTGNSLTSERKKEIYELARKYDFLIIEDDPYYFLQFNK
FRVPTFLSMDVDGRVIRADSFSKIISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQ
LMISQLLHEWGEEGFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKV
KGINDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMDVAFQVLAQL
IKESL
Enzyme 3 Number of Residues 425
Enzyme 3 Molecular Weight 47351.2
Enzyme 3 Theoretical pI 6.96
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthetic process
  • metabolic process
Component
Enzyme 3 General Function Transcription
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 63995206 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q4W5N8 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q4W5N8_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1278 bp
ATGAATTACGCACGGTTCATCACGGCAGCGAGCGCAGCCAGAAACCCTTCTCCCATCCGG
ACCATGACTGACATATTGAGCAGAGGACCAAAATCGATGATCTCCTTGGCTGGTGGCTTA
CCAAATCCAAACATGTTTCCTTTTAAGACTGCCGTAATCACTGTAGAAAATGGAAAGACC
ATCCAATTTGGAGAAGAGATGATGAAGAGAGCACTTCAGTATTCTCCGAGTGCTGGAATT
CCAGAGCTTTTGTCCTGGCTAAAACAGTTACAAATAAAATTGCATAATCCTCCTACCATC
CATTACCCACCCAGTCAAGGACAAATGGATCTATGTGTCACATCTGGCAGCCAACAAGGT
CTTTGTAAGGTGTTTGAAATGATCATTAATCCTGGAGATAATGTCCTCCTAGATGAACCT
GCTTATTCAGGAACTCTTCAAAGTCTGCACCCACTGGGCTGCAACATTATTAATGTTGCC
AGTGATGAAAGTGGGATTGTTCCAGATTCCCTAAGAGACATACTTTCCAGATGGAAACCA
GAAGATGCAAAGAATCCCCAGAAAAACACCCCCAAATTTCTTTATACTGTTCCAAATGGC
AACAACCCTACTGGAAACTCATTAACCAGTGAACGCAAAAAGGAAATCTATGAGCTTGCA
AGAAAATATGATTTCCTCATAATAGAAGATGATCCTTACTATTTTCTCCAGTTTAACAAG
TTCAGGGTACCAACATTTCTTTCCATGGATGTTGATGGACGTGTCATCAGAGCTGACTCT
TTTTCAAAAATCATTTCCTCTGGGTTGAGAATAGGATTTTTAACTGGTCCAAAACCCTTA
ATAGAGAGAGTTATTTTACACATACAAGTTTCAACATTGCACCCCAGCACTTTTAACCAG
CTCATGATATCACAGCTTCTACACGAATGGGGAGAAGAAGGTTTCATGGCTCATGTAGAC
AGGGTTATTGATTTCTATAGTAACCAGAAGGATGCAATACTGGCAGCTGCAGACAAGTGG
TTAACTGGTTTGGCAGAATGGCATGTTCCTGCTGCTGGAATGTTTTTATGGATTAAAGTT
AAAGGCATTAATGATGTAAAAGAACTGATTGAAGAAAAGGCCGTTAAGATGGGGGTATTA
ATGCTCCCTGGAAATGCTTTCTACGTCGATAGCTCAGCTCCTAGCCCTTACTTGAGAGCA
TCCTTCTCTTCAGCTTCTCCAGAACAGATGGATGTGGCCTTCCAGGTATTAGCACAACTT
ATAAAAGAATCTTTATGA
Enzyme 3 GenBank Gene ID AC084866 Link Image
Enzyme 3 GeneCard ID AADAT Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location 4
Enzyme 3 Locus 4q33
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 14844
Enzyme 4 Name 2-oxoglutarate dehydrogenase-like, mitochondrial
Enzyme 4 Synonyms
  1. 2-oxoglutarate dehydrogenase complex component E1-like
  2. OGDC-E1-like
  3. Alpha-ketoglutarate dehydrogenase-like
Enzyme 4 Gene Name OGDHL
Enzyme 4 Protein Sequence >2-oxoglutarate dehydrogenase-like, mitochondrial
MSQLRLLPSRLGVQAARLLAAHDVPVFGWRSRSSGPPATFPSSKGGGGSSYMEEMYFAWL
ENPQSVHKSWDSFFREASEEAFSGSAQPRPPSVVHESRSAVSSRTKTSKLVEDHLAVQSL
IRAYQIRGHHVAQLDPLGILDADLDSFVPSDLITTIDKLAFYDLQEADLDKEFQLPTTTF
IGGSENTLSLREIIRRLENTYCQHIGLEFMFINDVEQCQWIRQKFETPGVMQFSSEEKRT
LLARLVRSMRFEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMGIENVILGMPHRG
RLNVLANVIRKDLEQIFCQFDPKLEAADEGSGDVKYHLGMYHERINRVTNRNITLSLVAN
PSHLEAVDPVVQGKTKAEQFYRGDAQGKKVMSILVHGDAAFAGQGVVYETFHLSDLPSYT
TNGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNADDPEAVIYVCSVAAEW
RNTFNKDVVVDLVCYRRRGHNEMDEPMFTQPLMYKQIHRQVPVLKKYADKLIAEGTVTLQ
EFEEEIAKYDRICEEAYGRSKDKKILHIKHWLDSPWPGFFNVDGEPKSMTCPATGIPEDM
LTHIGSVASSVPLEDFKIHTGLSRILRGRADMTKNRTVDWALAEYMAFGSLLKEGIHVRL
SGQDVERGTFSHRHHVLHDQEVDRRTCVPMNHLWPDQAPYTVCNSSLSEYGVLGFELGYA
MASPNALVLWEAQFGDFHNTAQCIIDQFISTGQAKWVRHNGIVLLLPHGMEGMGPEHSSA
RPERFLQMSNDDSDAYPAFTKDFEVSQLYDCNWIVVNCSTPANYFHVLRRQILLPFRKPL
IIFTPKSLLRHPEAKSSFDQMVSGTSFQRVIPEDGAAARAPEQVQRLIFCTGKVYYDLVK
ERSSQDLEEKVAITRLEQISPFPFDLIKQEAEKYPGAELAWCQEEHKNMGYYDYISPRFM
TILRRARPIWYVGRDPAAAPATGNRNTHLVSLKKFLDTAFNLQAFEGKTF
Enzyme 4 Number of Residues 1010
Enzyme 4 Molecular Weight 114480.3
Enzyme 4 Theoretical pI 6.63
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
  • oxoglutarate dehydrogenase (succinyl-transferring) activity
  • thiamin pyrophosphate binding
  • vitamin binding
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 4 General Function Involved in oxoglutarate dehydrogenase (succinyl-transferring) activity
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 221316661 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9ULD0 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name OGDHL_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >3033 bp
ATGAGTCAGCTGAGGCTGCTGCCGTCCCGTCTTGGGGTACAGGCTGCGAGGCTCCTGGCT
GCACATGACGTCCCGGTGTTTGGCTGGCGCAGCAGGTCCTCCGGGCCACCGGCCACCTTC
CCAAGCAGCAAAGGTGGAGGCGGCTCCAGTTACATGGAGGAGATGTACTTCGCCTGGTTG
GAAAACCCCCAGAGTGTCCACAAGTCCTGGGACAGCTTCTTCAGGGAAGCCAGCGAGGAA
GCCTTTTCTGGCTCTGCTCAGCCACGGCCCCCTTCTGTTGTCCATGAGAGCAGGTCTGCA
GTCTCAAGTCGGACCAAGACCAGCAAATTGGTGGAGGACCACCTGGCTGTGCAGTCCCTG
ATCCGGGCCTACCAGATCCGGGGTCACCATGTGGCCCAGCTGGACCCCCTGGGCATTCTG
GATGCAGACCTGGACTCCTTTGTGCCCTCAGACTTGATCACAACCATTGATAAACTGGCC
TTCTATGACCTTCAGGAGGCTGACCTTGATAAGGAGTTCCAGCTGCCGACAACCACCTTC
ATTGGGGGCTCTGAAAACACCCTCTCTCTGCGGGAGATCATTCGGCGCCTGGAGAACACC
TACTGCCAGCACATTGGCCTGGAGTTCATGTTCATCAACGATGTGGAGCAGTGCCAGTGG
ATCCGGCAGAAGTTTGAGACCCCTGGTGTGATGCAGTTCTCCAGCGAGGAGAAGCGGACC
CTGCTGGCCCGGCTAGTGCGCTCCATGAGGTTTGAAGACTTCCTGGCCCGGAAATGGTCC
TCAGAGAAGCGGTTTGGCCTGGAGGGCTGTGAAGTGATGATTCCTGCCCTCAAGACCATC
ATCGACAAATCCAGCGAGATGGGGATTGAGAATGTCATCTTGGGGATGCCACACAGGGGA
AGGCTGAACGTGCTGGCCAACGTGATCCGCAAGGACCTGGAGCAGATCTTCTGCCAGTTT
GACCCCAAGCTGGAGGCGGCGGACGAGGGCTCCGGGGATGTCAAGTACCACCTGGGCATG
TACCATGAGAGGATCAACCGCGTCACCAACCGGAACATCACTCTGTCGCTGGTTGCCAAC
CCCTCCCACCTGGAGGCAGTGGACCCTGTGGTGCAGGGGAAGACAAAGGCAGAGCAGTTC
TACCGTGGAGATGCCCAGGGCAAGAAGGTCATGTCCATCCTGGTTCATGGGGACGCCGCC
TTTGCTGGCCAGGGCGTGGTATATGAGACCTTCCACCTGAGCGACCTGCCCTCCTACACG
ACCAATGGTACCGTGCACGTCGTCGTCAACAACCAGATTGGATTCACCACAGACCCCCGA
ATGGCCCGCTCCTCACCATACCCGACCGACGTGGCCCGGGTGGTCAATGCGCCTATCTTC
CATGTGAATGCCGATGACCCAGAGGCTGTGATATATGTGTGCAGTGTGGCAGCCGAATGG
AGAAACACTTTCAACAAAGATGTTGTCGTGGACCTGGTCTGTTACCGCCGGCGTGGCCAC
AATGAGATGGACGAGCCCATGTTCACCCAGCCGCTCATGTACAAGCAGATCCACAGACAG
GTGCCTGTGCTGAAGAAGTACGCAGACAAGCTGATTGCCGAGGGCACAGTCACCCTGCAG
GAGTTTGAGGAAGAAATTGCCAAATACGACCGGATCTGTGAGGAGGCTTATGGCAGGTCC
AAGGATAAAAAGATTCTGCATATAAAGCACTGGTTGGACTCCCCCTGGCCTGGCTTCTTC
AACGTAGATGGGGAGCCCAAGAGCATGACATGCCCAGCCACGGGGATCCCTGAGGACATG
CTCACCCACATCGGCAGTGTGGCCAGCTCTGTGCCCCTGGAGGACTTTAAGATCCACACT
GGCCTCTCTCGCATTCTGCGGGGCCGTGCGGACATGACCAAGAACCGGACGGTGGACTGG
GCGTTGGCAGAGTACATGGCCTTTGGCTCCCTGCTGAAGGAAGGCATCCACGTGCGGCTC
AGCGGGCAGGATGTGGAGAGGGGCACATTCAGTCACCGGCACCATGTTCTCCATGACCAG
GAGGTTGACCGCAGGACGTGTGTGCCTATGAATCATCTCTGGCCTGACCAGGCCCCGTAC
ACCGTGTGCAACAGCTCCCTCTCGGAGTACGGAGTCCTGGGCTTTGAGCTGGGCTATGCC
ATGGCCAGCCCCAATGCCCTGGTCCTCTGGGAGGCCCAGTTTGGGGACTTCCACAACACG
GCCCAGTGCATCATCGACCAGTTCATCAGCACCGGCCAGGCCAAGTGGGTGCGGCATAAT
GGCATTGTGCTGCTGCTGCCCCATGGCATGGAAGGCATGGGCCCAGAGCACTCGTCAGCG
AGGCCCGAAAGGTTCCTGCAGATGAGCAATGATGACTCGGATGCCTACCCTGCATTCACC
AAGGACTTCGAGGTGAGCCAGCTCTATGACTGCAACTGGATCGTGGTCAACTGCTCCACA
CCGGCCAACTACTTCCACGTGCTGCGCCGGCAGATCCTGCTGCCCTTCCGCAAGCCGCTG
ATTATCTTCACACCTAAATCTCTGCTGAGGCACCCAGAGGCCAAGTCCAGCTTTGACCAA
ATGGTATCCGGGACCAGCTTCCAGCGGGTGATTCCTGAAGATGGGGCCGCAGCACGGGCC
CCTGAGCAGGTGCAGCGGCTCATCTTCTGCACGGGAAAGGTGTACTATGACCTGGTGAAG
GAGCGGAGCAGCCAGGACCTGGAGGAGAAAGTGGCCATCACGCGCCTGGAGCAGATCTCT
CCATTCCCCTTCGACCTGATCAAGCAGGAGGCAGAGAAGTACCCAGGTGCGGAGCTGGCC
TGGTGTCAGGAGGAGCACAAGAACATGGGCTACTATGACTACATCAGCCCACGCTTCATG
ACCATCCTGAGGCGCGCACGGCCCATATGGTATGTTGGCCGGGACCCAGCGGCTGCACCA
GCCACAGGAAACAGGAACACTCACCTGGTGTCACTGAAGAAGTTTCTGGATACTGCCTTC
AATCTCCAGGCCTTTGAGGGCAAGACATTTTAG
Enzyme 4 GenBank Gene ID NM_018245.2 Link Image
Enzyme 4 GeneCard ID OGDHL Link Image
Enzyme 4 GenAtlas ID OGDHL Link Image
Enzyme 4 HGNC ID HGNC:25590 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 10q11.23
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [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. 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 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 16512
Enzyme 5 Name Putative uncharacterized protein
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name DLD
Enzyme 5 Protein Sequence >Putative uncharacterized protein
MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKA
AQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNL
DKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNIL
IATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVT
AVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGK
AEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGP
MLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGK
FPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDI
ARVCHAHPTLSEAFREANLAASFGKSINF
Enzyme 5 Number of Residues 509
Enzyme 5 Molecular Weight 54178
Enzyme 5 Theoretical pI 7.95
Enzyme 5 GO Classification
Function
  • FAD binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • dihydrolipoyl dehydrogenase activity
  • disulfide oxidoreductase activity
  • electron transporter activity
  • nucleotide binding
  • oxidoreductase activity
  • purine nucleotide binding
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 5 General Function Energy production and conversion
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID B2R5X0 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name B2R5X0_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK312346 Link Image
Enzyme 5 GeneCard ID B2R5X0 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available