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Human Metabolome Database Version 2.5

 

Showing metabocard for 1-Methylnicotinamide (HMDB00699)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-07-30 13:58:04
Accession Number HMDB00699
Secondary Accession Numbers Not Available
Common Name 1-Methylnicotinamide
Description 1-Methylnicotinamide is a metabolite of nicotinamide and is produced primarily in the liver. It has anti-inflammatory properties (PMID 16197374). It is a product of nicotinamide N-methyltransferase [EC 2.1.1.1] in the pathway of nicotinate and nicotinamide metabolism (KEGG). 1-Methylnicotinamide may be an endogenous activator of prostacyclin production and thus may regulate thrombotic as well as inflammatory processes in the cardiovascular system (PMID: 17641676).
Synonyms
  1. 1-Methyl-3-carbamoylpyridinium
  2. 1-Methyl-3-carbamoylpyridinium cation
  3. 1-Methylnicotinamide
  4. I-methyl nicotinamide
  5. 3-Amido-N-methylpyridinium: 1-methyl-3-Pyridinecarboxamide
  6. 3-carbamoyl-1-methyl-Pyridinium
  7. N'-methylnicotinamide
  8. N'methylnicotinamide
  9. N-Methyl-3-carbamidopyridinium
  10. N-Methyl-3-carbamoylpyridinium ion
  11. N1-Methylnicotinamide
  12. N-1-methylnicotinamide
  13. Trigonellinamide
Chemical IUPAC Name 1-methylpyridin-1-ium-3-carboxamide
Chemical Formula C7H9N2O
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Ketones and Aldehydes
Class
  • Amino Ketones
Sub Class
  • Aliphatic amides
Family
  • Mammalian Metabolite
Species
  • cation
  • primary carboxylic acid amide
  • aromatic compound
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 137.159
Monoisotopic Molecular Weight 137.071487
Isomeric SMILES C[N+]1=CC=CC(=C1)C(N)=O
Canonical SMILES C[N+]1=CC=CC(=C1)C(N)=O
KEGG Compound ID C02918 Link Image
BioCyc ID CPD-396 Link Image
BiGG ID 2226225 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB00699 Link Image
Metagene Link HMDB00699 Link Image
METLIN ID 5667 Link Image
PubChem Compound 457 Link Image
PubChem Substance 2394 Link Image
ChEBI ID 16797 Link Image
CAS Registry Number 3106-60-3
InChI Identifier InChI=1/C7H8N2O/c1-9-4-2-3-6(5-9)7(8)10/h2-5H,1H3,(H-,8,10)/p+1
Synthesis Reference Nelis, Hans J. C. F.; Airy, Subhash C.; Sinsheimer, J. E. Comparison of the alkylation of nicotinamide and 4-(p-nitrobenzyl)pyridine for the determination of aliphatic epoxides. Analytical Chemistry (1982), 54(2), 213-16.
Melting Point (Experimental) Not Available
Experimental Water Solubility 855 mg/mL [Chloride salt, HMP experimental] Source: PhysProp
Predicted Water Solubility 0.725 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -3.72 [Predicted by ALOGPS]; 0.757 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
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 Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • Extracellular
Biofluid Location
  • Blood
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 0.430 (0.007-0.850) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Musfeld C, Biollaz J, Belaz N, Kesselring UW, Decosterd LA: Validation of an HPLC method for the determination of urinary and plasma levels of N1-methylnicotinamide, an endogenous marker of renal cationic transport and plasma flow. J Pharm Biomed Anal. 2001 Jan;24(3):391-404. [PubMed Link Image]
Biofluid Urine
Value 6.105 (0.240-12.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Musfeld C, Biollaz J, Belaz N, Kesselring UW, Decosterd LA: Validation of an HPLC method for the determination of urinary and plasma levels of N1-methylnicotinamide, an endogenous marker of renal cationic transport and plasma flow. J Pharm Biomed Anal. 2001 Jan;24(3):391-404. [PubMed Link Image]
Biofluid Urine
Value 0.82 (0.26-2.3) umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 1.9 (0.67-5.1) umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 3.5 (1.3-6.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 4.8 (1.86-13.94) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 2.5 (2.1-2.8) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Creeke PI, Dibari F, Cheung E, van den Briel T, Kyroussis E, Seal AJ: Whole blood NAD and NADP concentrations are not depressed in subjects with clinical pellagra. J Nutr. 2007 Sep;137(9):2013-7. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.130 (0.045-0.850) uM
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
  • Somogyi A, Siebert D, Bochner F: Determination of endogenous concentrations of N1-methylnicotinamide in human plasma and urine by high-performance liquid chromatography. Anal Biochem. 1990 May 15;187(1):160-5. [PubMed Link Image]
Biofluid Urine
Value 3.0 (0.0-14.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Lung Cancer
Comments Not Available
References
  • HMP Experimental
Biofluid Urine
Value 37.00 (11.5-62.7) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Pellagra
Comments Not Available
References
  • Creeke PI, Dibari F, Cheung E, van den Briel T, Kyroussis E, Seal AJ: Whole blood NAD and NADP concentrations are not depressed in subjects with clinical pellagra. J Nutr. 2007 Sep;137(9):2013-7. [PubMed Link Image]
Associated Disorders
Condition References
Lung Cancer
  • HMP Experimental
Pellagra
  • Creeke PI, Dibari F, Cheung E, van den Briel T, Kyroussis E, Seal AJ: Whole blood NAD and NADP concentrations are not depressed in subjects with clinical pellagra. J Nutr. 2007 Sep;137(9):2013-7. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Nicotinate and Nicotinamide Metabolism SMP00048 Link Image map00760 Link Image
General References
  1. Pelletier O, Brassard R: Automated and manual determination of N1-methylnicotinamide in urine. Am J Clin Nutr. 1977 Dec;30(12):2108-16. [PubMed Link Image]
  2. Carter EG: Quantitation of urinary niacin metabolites by reversed-phase liquid chromatography. Am J Clin Nutr. 1982 Nov;36(5):926-30. [PubMed Link Image]
  3. Slominska EM, Smolenski RT, Szolkiewicz M, Leaver N, Rutkowski B, Simmonds HA, Swierczynski J: Accumulation of plasma N-methyl-2-pyridone-5-carboxamide in patients with chronic renal failure. Mol Cell Biochem. 2002 Feb;231(1-2):83-8. [PubMed Link Image]
  4. Ohdoi C, Nyhan WL, Kuhara T: Chemical diagnosis of Lesch-Nyhan syndrome using gas chromatography-mass spectrometry detection. J Chromatogr B Analyt Technol Biomed Life Sci. 2003 Jul 15;792(1):123-30. [PubMed Link Image]
  5. Patterson JI, Brown RR, Linkswiler H, Harper AE: Excretion of tryptophan-niacin metabolites by young men: effects of tryptophan, leucine, and vitamin B6 intakes. Am J Clin Nutr. 1980 Oct;33(10):2157-67. [PubMed Link Image]
  6. Musfeld C, Biollaz J, Belaz N, Kesselring UW, Decosterd LA: Validation of an HPLC method for the determination of urinary and plasma levels of N1-methylnicotinamide, an endogenous marker of renal cationic transport and plasma flow. J Pharm Biomed Anal. 2001 Jan;24(3):391-404. [PubMed Link Image]
Metabolic Enzymes
  1. Aldehyde oxidase
  2. Nicotinamide N-methyltransferase
  3. Aldeyde oxidase
Enzyme 1 [top]
Enzyme 1 ID 5358
Enzyme 1 Name Aldehyde oxidase
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name AOX1
Enzyme 1 Protein Sequence >Aldehyde oxidase 
MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTPYGCGGGGCGACTVMISRYN
PITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPG
MVMSIYPLLRNHPEPTLDQLTDALGGNLCRCHGYRPIIDACKTFCKTSGCCQSKENGVCC
LDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMADKQSQRTRVFGSER
MMWFSPVTLKDLLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPGYNSPDRIEEPECCKPC
IYGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHII
SRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPISR
KWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKL
IGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPV
HYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYC
DDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAE
KFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPE
RKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKY
IQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGE
DMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKF
PNLRCRGWACRTNLPSNTAFRGFGFPQAVLITESCITEVAAKCGLSPEKVRIINMYKEID
QTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLAS
RAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETV
PNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVG
YFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAID
IGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSN
TLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFT
KMIPRDEPGSYVPWNVPI
Enzyme 1 Number of Residues 1338
Enzyme 1 Molecular Weight 147933
Enzyme 1 Theoretical pI 7.11
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron transporter activity
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Nucleotide transport and metabolism
Enzyme 1 Specific Function An aldehyde + H(2)O + O(2) = a carboxylic acid + H(2)O(2)
Enzyme 1 Pathways
Enzyme 1 Reactions
  • an aldehyde + H2O + O2 = a carboxylic acid + H2O2
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 438656 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q06278 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ADO_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >4017 bp 
ATGGACCGGGCGTCCGAGCTGCTCTTCTACGTGAACGGCCGCAAGGTGATAGAAAAAAAT
GTCGATCCTGAAACAATGCTGTTGCCTTATTTGAGGAAGAAGCTTCGACTCACAGGAACT
CCGTATGGCTGTGGAGGAGGAGGCTGTGGTGCTTGTACAGTGATGATATCACGATACAAC
CCCATCACCAAGAGGATAAGGCATCACCCAGCCAATGCCTGTCTGATTCCCATCTGTTCT
CTGTATGGTGCTGCCGTCACCACAGTAGAAGGCATAGGAAGCACCCACACCAGAATTCAT
CCTGTTCAGGAGAGGATTGCCAAGTGTCATGGCACCCAGTGTGGCTTCTGCACACCTGGG
ATGGTGATGTCCATCTACCCCCTGCTCAGGAACCACCCAGAGCCCACTCTGGATCAGTTA
ACTGATGCCCTTGGTGGTAACCTGTGCCGTTGCCATGGATACAGGCCCATAATTGATGCA
TGCAAGACTTTCTGTAAAACTTCGGGCTGCTGTCAAAGTAAAGAAAATGGGGTTTGCTGT
TTGGATCAAGGAATCAATGGATTGCCAGAATTTGAGGAAGGAAGTAAGACAAGTCCAAAA
CTCTTCGCAGAAGAGGAGTTTCTGCCATTGGATCCAACCCAGGAACTGATATTTCCTCCT
GAGCTAATGATAATGGCTGATAAACAGTCGCAAAGGACCAGGGTGTTTGGCAGTGAGAGA
ATGATGTGGTTTTCCCCCGTGACCCTGAAGGACCTGCTGGAATTTAAATTCAAGTATCCC
CAGGCTCCTGTTATCATGGGAAACACCTCTGTGGGGCCTGAAGTGAAATTTAAAGGCGTC
TTTCACCCAGGTTATAATTCTCCTGATAGAATTGAAGAACCTGAGTGTTGTAAACCATGC
ATATATGGACTCACCCTTGGTGCTGGTCTCAGCCTAGCCCAGGTGAAGGACATTTTGGCT
GATGTAGTCCAGAAGCTTCCAGAGGAGAAGACACAGATGTACCATGCTCTCCTGAAGCAT
TTGGGAACTCTGGCTGGGTCCCAGATCAGGAACATGGCTTCTTTAGGGGGACACATCATT
AGCAGGCATCCAGATTCAGATCTGAATCCCATCCTGGCTGTGGGTAACTGTACCCTCAAC
TTGCTATCAAAAGAAGGAAAACGACAGATTCCTTTAAATGAGCAATTCCTCAGCAAGTGC
CCTAATGCAGATCTTAAGCCTCAAGAAATCTTGGTCTCAGTGAACATCCCCATCTCAAGG
AAGTGGGAATTTGTGTCAGCCTTCCGACAAGCCCAGCGACAGGAGAATGCGCTAGCGATA
GTCAATTCAGGAATGAGAGTCTTTTTTGGAGAAGGGGATGGCATTATTAGAGAGTTATGC
ATCTCATATGGAGGCGTTGGTCCAGCCACCATCTGTGCCAAGAATTCCTGCCAGAAACTC
ATTGGAAGGCACTGGAACGAACAGATGCTGGATATAGCCTGCAGGCTTATTCTGAATGAA
GTCTCCCTTTTGGGCTCGGCGCCAGGTGGGAAAGTGGAGTTCAAGAGGACTCTCATCATC
AGCTTCCTCTTCAAGTTCTACCTGGAAGTGTCACAGATTTTGAAAAAGATGGATCCAGTT
CACTATCCTAGCCTTGCAGACAAGTATGAAAGTGCTTTAGAAGATCTTCATTCCAAACAT
CACTGCAGTACATTAAAGTACCAGAATATAGGCCCAAAGCAGCATCCTGAAGACCCAATT
GGCCACCCCATCATGCATCTGTCTGGTGTGAAGCATGCCACGGGGGAGGCCATCTACTGT
GATGACATGCCTCTGGTGGACCAGGAACTTTTCTTGACTTTTGTGACTAGTTCAAGAGCT
CATGCTAAGATTGTGTCTATTGATCTGTCAGAAGCTCTCAGCATGCCCGGTGTGGTGGAC
ATCATGACAGCAGAACATCTTAGTGACGTCAACTCCTTCTGCTTTTTTACTGAAGCTGAG
AAATTTCTGGCGACAGATAAGGTGTTCTGTGTGGGTCAGCTTGTCTGTGCTGTGCTTGCC
GATTCTGAGGTTCAGGCAAAGCGAGCTGCTAAGCGAGTGAAGATTGTCTATCAAGACTTG
GAGCCGCTGATACTAACAATTGAGGAAAGTATACAACACAACTCCTCCTTCAAGCCAGAA
AGGAAACTGGAATATGGAAATGTTGACGAAGCATTTAAAGTGGTTGATCAAATTCTTGAA
GGTGAAATACATATGGGAGGTCAAGAACATTTTTATATGGAAACCCAAAGCATGCTTGTC
GTTCCCAAGGGAGAGGATCAAGAAATGGATGTCTACGTGTCCACACAGTTTCCCAAATAT
ATACAGGACATTGTTGCCTCAACCTTGAAGCTCCCAGCTAACAAGGTCATGTGCCATGTA
AGGCGTGTTGGTGGAGCGTTTGGAGGGAAGGTGTTAAAAACCGGAATCATTGCAGCCGTC
ACTGCATTTGCCGCAAACAAACATGGCCGTGCAGTTCGCTGTGTTCTGGAACGAGGAGAA
GACATGTTAATAACTGGAGGCCGCCATCCTTACCTTGGAAAGTACAAAGCTGGATTCATG
AACGATGGCAGAATCTTGGCCCTGGACATGGAGCATTACAGCAATGCAGGCGCCTCCTTG
GATGAATCATTATTCGTGATAGAAATGGGACTTCTGAAAATGGACAATGCTTACAAGTTT
CCCAATCTCCGCTGCCGGGGTTGGGCATGCAGAACCAACCTTCCATCCAACACAGCTTTT
CGTGGGTTTGGCTTTCCTCAGGCAGTGCTGATCACCGAATCTTGTATCACGGAAGTTGCA
GCCAAATGTGGACTATCCCCTGAGAAGGTGCGAATCATAAACATGTACAAGGAAATTGAT
CAAACACCCTACAAACAAGAGATCAATGCCAAGAACCTAATCCAGTGTTGGAGAGAATGT
ATGGCCATGTCTTCCTACTCCTTGAGGAAAGTTGCTGTGGAAAAGTTCAATGCAGAGAAT
TATTGGAAGAAGAAAGGACTGGCCATGGTCCCCCTGAAGTTTCCTGTTGGCCTTGCGTCA
CGTGCTGCTGGTCAGGCTGCTGCCTTGGTTCACATTTATCTTGATGGCTCTGTGCTGGTC
ACTCACGGTGGAATTGAAATGGGGCAGGGGGTCCACACTAAAATGATTCAGGTGGTCAGC
CGTGAATTAAGAATGCCAATGTCGAATGTCCACCTGCGTGGAACAAGCACAGAAACTGTC
CCTAATGCAAATATCTCTGGAGGTTCTGTGGTGGCAGATCTCAACGGTTTGGCAGTAAAG
GATGCCTGTCAAACTCTTCTAAAACGCCTCGAACCCATCATCAGCAAGAATCCTAAAGGA
ACTTGGAAAGACTGGGCACAGACTGCTTTTGATGAAAGCATTAACCTTTCAGCTGTTGGA
TACTTCAGAGGTTATGAGTCAGACATGAACTGGGAGAAAGGCGAAGGCCAGCCCTTCGAA
TACTTTGTTTATGGAGCTGCCTGTTCCGAGGTTGAAATAGACTGCCTGACGGGGGATCAT
AAGAACATCAGAACAGACATTGTCATGGATGTTGGCTGCAGTATAAATCCAGCCATTGAC
ATAGGCCAGATTGAAGGTGCATTTATTCAAGGCATGGGACTTTATACAATAGAGGAACTG
AATTATTCTCCCCAGGGCATTCTGCACACTCGTGGTCCAGACCAATATAAAATCCCTGCC
ATCTGTGACATGCCCACGGAGTTGCACATTGCTTTGTTGCCTCCTTCTCAAAACTCAAAT
ACTCTTTATTCATCTAAGGGTCTGGGAGAGTCGGGGGTGTTCCTGGGGTGTTCCGTGTTT
TTCGCTATCCATGACGCAGTGAGTGCAGCACGACAGGAGAGAGGCCTGCATGGACCCTTG
ACCCTTAATAGTCCACTGACCCCGGAGAAGATTAGGATGGCCTGTGAAGACAAGTTCACA
AAAATGATTCCGAGAGATGAACCTGGATCCTACGTTCCTTGGAATGTACCCATCTGA
Enzyme 1 GenBank Gene ID L11005 Link Image
Enzyme 1 GeneCard ID AOX1 Link Image
Enzyme 1 GenAtlas ID AOX1 Link Image
Enzyme 1 HGNC ID HGNC:553 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2q33
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Wright RM, Vaitaitis GM, Wilson CM, Repine TB, Terada LS, Repine JE: cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10690-4. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5660
Enzyme 2 Name Nicotinamide N-methyltransferase
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name NNMT
Enzyme 2 Protein Sequence >Nicotinamide N-methyltransferase 
MESGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLI
DIGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGN
RVKGPEKEEKLRQAVKQVLKCDVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRAL
RNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQ
SYSSTMANNEGLFSLVARKLSRPL
Enzyme 2 Number of Residues 264
Enzyme 2 Molecular Weight 29574
Enzyme 2 Theoretical pI 5.45
Enzyme 2 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
—
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is important for biotransformation of many drugs and xenobiotic compounds
Enzyme 2 Pathways
  • Nicotinate and Nicotinamide Metabolism (map00760 Link Image)
Enzyme 2 Reactions
  • S-adenosyl-L-methionine + nicotinamide = S-adenosyl-L-homocysteine + 1-methylnicotinamide
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 494989 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P40261 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name NNMT_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >795 bp 
ATGGAATCAGGCTTCACCTCCAAGGACACCTATCTAAGCCATTTTAACCCTCGGGATTAC
CTAGAAAAATATTACAAGTTTGGTTCTAGGCACTCTGCAGAAAGCCAGATTCTTAAGCAC
CTTCTGAAAAATCTTTTCAAGATATTCTGCCTAGACGGTGTGAAGGGAGACCTGCTGATT
GACATCGGCTCTGGCCCCACTATCTATCAGCTCCTCTCTGCTTGTGAATCCTTTAAGGAG
ATCGTCGTCACTGACTACTCAGACCAGAACCTGCAGGAGCTGGAGAAGTGGCTGAAGAAA
GAGCCAGAGGCCTTTGACTGGTCCCCAGTGGTGACCTATGTGTGTGATCTTGAAGGGAAC
AGAGTCAAGGGTCCAGAGAAGGAGGAGAAGTTGAGACAGGCGGTCAAGCAGGTGCTGAAG
TGTGATGTGACTCAGAGCCAGCCACTGGGGGCCGTCCCCTTACCCCCGGCTGACTGCGTG
CTCAGCACACTGTGTCTGGATGCCGCCTGCCCAGACCTCCCCACCTACTGCAGGGCGCTC
AGGAACCTCGGCAGCCTACTGAAGCCAGGGGGCTTCCTGGTGATCATGGATGCGCTCAAG
AGCAGCTACTACATGATTGGTGAGCAGAAGTTCTCCAGCCTCCCCCTGGGCCGGGAGGCA
GTAGAGGCTGCTGTGAAAGAGGCTGGCTACACAATCGAATGGTTTGAGGTGATCTCGCAA
AGTTATTCTTCCACCATGGCCAACAACGAAGGACTTTTCTCCCTGGTGGCGAGGAAGCTG
AGCAGACCCCTGTGA
Enzyme 2 GenBank Gene ID U08021 Link Image
Enzyme 2 GeneCard ID NNMT Link Image
Enzyme 2 GenAtlas ID NNMT Link Image
Enzyme 2 HGNC ID HGNC:7861 Link Image
Enzyme 2 Chromosome Location 11
Enzyme 2 Locus 11q23.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Aksoy S, Szumlanski CL, Weinshilboum RM: Human liver nicotinamide N-methyltransferase. cDNA cloning, expression, and biochemical characterization. J Biol Chem. 1994 May 20;269(20):14835-40. [PubMed Link Image]
  2. Aksoy S, Brandriff BF, Ward A, Little PF, Weinshilboum RM: Human nicotinamide N-methyltransferase gene: molecular cloning, structural characterization and chromosomal localization. Genomics. 1995 Oct 10;29(3):555-61. [PubMed Link Image]
  3. Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 13071
Enzyme 3 Name Aldeyde oxidase
Enzyme 3 Synonyms
  1. Aldehyde oxidase 1, isoform CRA_b
  2. Aldehyde oxidase 1
Enzyme 3 Gene Name hAO
Enzyme 3 Protein Sequence >Aldeyde oxidase 
MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYN
PITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPG
MVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKTSGCCQSKENGVCC
LDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMAEKQSQRTRVFGSER
MMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHA
YNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHII
SRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSR
KWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKL
IGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPV
HYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYC
DDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAE
KFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPE
RKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKY
IQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGE
DMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKF
PNLRCRGWACRTNLPSNTAFRGFGFPQAALITESCITEVAAKCGLSPEKVRIINMYKEID
QTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLGS
RAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETV
PNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVG
YFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAID
IGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSN
TLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFT
KMIPRDEPGSYVPWNVPI
Enzyme 3 Number of Residues 1338
Enzyme 3 Molecular Weight 147920
Enzyme 3 Theoretical pI 7.17
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron transporter activity
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Nucleotide transport and metabolism
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways
Enzyme 3 Reactions
  • an aldehyde + H2O + O2 = a carboxylic acid + H2O2 [RN:R00635] ALL_REAC R00635 > R02657 R04904
  • (other) R01709 R02655 R03871 R04085
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 109658814 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9BYF0 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q9BYF0_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID BC117179 Link Image
Enzyme 3 GeneCard ID Q9BYF0 Link Image
Enzyme 3 GenAtlas ID hAO Link Image
Enzyme 3 HGNC ID HGNC:553 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Ichida K, Matsumura T, Sakuma R, Hosoya T, Nishino T: Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II. Biochem Biophys Res Commun. 2001 Apr 20;282(5):1194-200. [PubMed Link Image]
  2. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available