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Human Metabolome Database Version 2.5

 

Showing metabocard for S-Adenosylmethioninamine (HMDB00988)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:25
Accession Number HMDB00988
Secondary Accession Numbers Not Available
Common Name S-Adenosylmethioninamine
Description S-Adenosylmethioninamine is a biological sulfonium compound known as the major biological methyl donor. It is also a donor of methylene groups, amino groups, ribosyl groups and aminopropyl groups (PMID 15130560). S-Adenosylmethioninamine is a prodcut of enzyme adenosylmethionine decarboxylase [EC 4.1.1.50] in methionine metabolism pathway (KEGG).
Synonyms
  1. (5-deoxy-5-adenosyl)(3-aminopropyl) methylsulfonium salt
  2. S-Adenosyl-L-methioninamine
  3. S-adenosylmethioninamine
  4. dAdoMet
  5. decarboxylated AdoMet
  6. decarboxylated S-adenosylmethionine
  7. decarboxylated SAM
Chemical IUPAC Name 3-aminopropyl-[[5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methyl]-methyl-sulfonium
Chemical Formula C14H23N6O3S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleoside Analogues
Sub Class
  • Methylated nucleosides
Family
  • Mammalian Metabolite
Species
  • cation
  • secondary alcohol
  • 1,2-diol
  • primary amine
  • primary aliphatic amine (alkylamine)
  • primary aromatic amine
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Arginine and proline metabolism
  • Component of beta-Alanine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 355.436
Monoisotopic Molecular Weight 355.155243
Isomeric SMILES C[S+](CCCN)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC2=C1N=CN=C2N
Canonical SMILES C[S+](CCCN)CC1OC(C(O)C1O)N1C=NC2=C1N=CN=C2N
KEGG Compound ID C01137 Link Image
BioCyc ID S-ADENOSYLMETHIONINAMINE Link Image
BiGG ID 36895 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB00988 Link Image
Metagene Link HMDB00988 Link Image
METLIN ID 3501 Link Image
PubChem Compound 1078 Link Image
PubChem Substance 3154 Link Image
ChEBI ID 15625 Link Image
CAS Registry Number 22365-13-5
InChI Identifier InChI=1/C14H23N6O3S/c1-24(4-2-3-15)5-8-10(21)11(22)14(23-8)20-7-19-9-12(16)17-6-18-13(9)20/h6-8,10-11,14,21-22H,2-5,15H2,1H3,(H2,16,17,18)/q+1/t8-,10-,11-,14-,24?/m1/s1
Synthesis Reference Pegg, Anthony E. Assay of aminopropyltransferases. Methods in Enzymology (1983), 94(Polyamines), 260-5.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.27 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.28 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
Biofluid Location
  • Cerebrospinal Fluid
Tissue Location Not Available
Concentrations (Normal)
Biofluid CSF
Value 0.207 +/- 0.037 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Linnebank M, Popp J, Smulders Y, Smith D, Semmler A, Farkas M, Kulic L, Cvetanovska G, Blom H, Stoffel-Wagner B, Kolsch H, Weller M, Jessen F: S-adenosylmethionine is decreased in the cerebrospinal fluid of patients with Alzheimer's disease. Neurodegener Dis. 2010;7(6):373-8. Epub 2010 Jun 3. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid CSF
Value 0.193 +/- 0.031 uM
Age Adult:>18 yrs old
Sex N/A
Comments Not Available
References
  • Linnebank M, Popp J, Smulders Y, Smith D, Semmler A, Farkas M, Kulic L, Cvetanovska G, Blom H, Stoffel-Wagner B, Kolsch H, Weller M, Jessen F: S-adenosylmethionine is decreased in the cerebrospinal fluid of patients with Alzheimer's disease. Neurodegener Dis. 2010;7(6):373-8. Epub 2010 Jun 3. [PubMed Link Image]
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Methionine Metabolism SMP00033 Link Image map00270 Link Image
Spermidine and Spermine Biosynthesis SMP00445 Link Image
General References
  1. Fontecave M, Atta M, Mulliez E: S-adenosylmethionine: nothing goes to waste. Trends Biochem Sci. 2004 May;29(5):243-9. [PubMed Link Image]
Metabolic Enzymes
  1. Spermine synthase
  2. Spermidine synthase
  3. Spermidine synthase (Spermidine synthase, isoform CRA_a)
  4. Adenosylmethionine decarboxylase 1
Enzyme 1 [top]
Enzyme 1 ID 5449
Enzyme 1 Name Spermine synthase
Enzyme 1 Synonyms
  1. SPMSY
  2. Spermidine aminopropyltransferase
Enzyme 1 Gene Name SMS
Enzyme 1 Protein Sequence >Spermine synthase
MAAARHSTLDFMLGAKADGETILKGLQSIFQEQGMAESVHTWQDHGYLATYTNKNGSFAN
LRIYPHGLVLLDLQSYDGDAQGKEEIDSILNKVEERMKELSQDSTGRVKRLPPIVRGGAI
DRYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRA
IMGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRKTCGDV
LDNLKGDCYQVLIEDCIPVLKRYAKEGREFDYVINDLTAVPISTSPEEDSTWEFLRLILD
LSMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTV
WKKAKP
Enzyme 1 Number of Residues 366
Enzyme 1 Molecular Weight 41267.9
Enzyme 1 Theoretical pI 4.62
Enzyme 1 GO Classification
Function
  • catalytic activity
  • spermine synthase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • metabolic process
  • polyamine biosynthetic process
  • polyamine metabolic process
  • spermine biosynthetic process
Component
Enzyme 1 General Function Involved in spermine synthase activity
Enzyme 1 Specific Function Required for normal viability, growth and fertility
Enzyme 1 Pathways
Enzyme 1 Reactions
  • S-adenosylmethioninamine + spermidine = S-methyl-5'-thioadenosine + spermine [RN:R02869]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 2198557 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P52788 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name SPSY_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1101 bp
ATGGCAGCAGCACGGCACAGCACGCTCGACTTCATGCTCGGCGCCAAAGCTGATGGTGAG
ACCATTCTAAAAGGCCTCCAGTCCATTTTCCAGGAGCAGGGGATGGCGGAGTCGGTGCAC
ACCTGGCAGGACCATGGCTATTTAGCAACCTACACAAACAAGAACGGCAGCTTTGCCAAT
TTGAGAATTTACCCACATGGATTGGTGTTGCTGGACCTTCAGAGTTATGATGGTGATGCG
CAAGGCAAAGAAGAGATCGACAGTATTTTGAACAAAGTAGAGGAAAGAATGAAAGAATTG
AGTCAGGACAGTACTGGGCGGGTGAAACGATTACCACCCATAGTGCGAGGAGGAGCCATC
GACAGATACTGGCCCACCGCCGACGGGCGCCTGGTTGAATATGACATAGATGAAGTGGTA
TATGACGAAGATTCACCTTATCAAAATATAAAAATTCTACACTCGAAGCAGTTTGGAAAT
ATTCTCATCCTTAGTGGGGATGTTAATTTGGCAGAGAGTGATTTGGCATATACCCGGGCC
ATCATGGGCAGTGGCAAAGAAGATTACACTGGCAAAGATGTACTCATTCTGGGAGGTGGA
GACGGAGGCATATTGTGTGAAATAGTCAAACTAAAACCAAAGATGGTCACTATGGTAGAG
ATTGACCAAATGGTGATTGATGGGTGTAAGAAATACATGCGAAAAACGTGTGGCGATGTC
TTAGACAATCTTAAAGGAGACTGCTATCAGGTTCTAATAGAAGACTGTATCCCGGTACTG
AAGAGGTACGCCAAAGAAGGGAGAGAATTTGATTATGTGATTAATGATTTGACAGCTGTT
CCAATCTCCACGTCTCCAGAAGAAGATTCCACATGGGAGTTTCTCAGACTGATTCTTGAC
CTCTCAATGAAAGTGTTGAAACAGGATGGGAAATATTTTACACAGGGGAACTGTGTCAAT
CTGACAGAAGCACTGTCGCTCTATGAAGAACAGCTGGGGCGCCTGTATTGTCCTGTGGAA
TTTTCAAAGGAGATCGTCTGTGTCCCTTCATACTTGGAATTGTGGGTATTTTACACTGTT
TGGAAGAAAGCTAAACCCTGA
Enzyme 1 GenBank Gene ID AD001528 Link Image
Enzyme 1 GeneCard ID SMS Link Image
Enzyme 1 GenAtlas ID SMS Link Image
Enzyme 1 HGNC ID HGNC:11123 Link Image
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Korhonen VP, Halmekyto M, Kauppinen L, Myohanen S, Wahlfors J, Keinanen T, Hyvonen T, Alhonen L, Eloranta T, Janne J: Molecular cloning of a cDNA encoding human spermine synthase. DNA Cell Biol. 1995 Oct;14(10):841-7. [PubMed Link Image]
  2. Grieff M, Whyte MP, Thakker RV, Mazzarella R: Sequence analysis of 139 kb in Xp22.1 containing spermine synthase and the 5' region of PEX. Genomics. 1997 Sep 1;44(2):227-31. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  5. 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]
  6. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  7. Cason AL, Ikeguchi Y, Skinner C, Wood TC, Holden KR, Lubs HA, Martinez F, Simensen RJ, Stevenson RE, Pegg AE, Schwartz CE: X-linked spermine synthase gene (SMS) defect: the first polyamine deficiency syndrome. Eur J Hum Genet. 2003 Dec;11(12):937-44. [PubMed Link Image]
  8. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  9. 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]
  10. Wu H, Min J, Zeng H, McCloskey DE, Ikeguchi Y, Loppnau P, Michael AJ, Pegg AE, Plotnikov AN: Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. J Biol Chem. 2008 Jun 6;283(23):16135-46. Epub 2008 Mar 26. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5450
Enzyme 2 Name Spermidine synthase
Enzyme 2 Synonyms
  1. SPDSY
  2. Putrescine aminopropyltransferase
Enzyme 2 Gene Name SRM
Enzyme 2 Protein Sequence >Spermidine synthase
MEPGPDGPAASGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYG
NVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESV
VQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGP
AESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFPVVAYAYCTIPT
YPSGQIGFMLCSKNPSTNFQEPVQPLTQQQVAQMQLKYYNSDVHRAAFVLPEFARKALND
VS
Enzyme 2 Number of Residues 302
Enzyme 2 Molecular Weight 33824.5
Enzyme 2 Theoretical pI 5.17
Enzyme 2 GO Classification
Function
  • catalytic activity
Process
Component
Enzyme 2 General Function Involved in catalytic activity
Enzyme 2 Specific Function S-adenosylmethioninamine + putrescine = 5'-S- methyl-5'-thioadenosine + spermidine
Enzyme 2 Pathways
Enzyme 2 Reactions
  • S-adenosylmethioninamine + putrescine = 5'-S-methyl-5'-thioadenosine + spermidine [RN:R01920]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 56204109 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P19623 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name SPEE_HUMAN Link Image
Enzyme 2 PDB ID 1ZDZ Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >909 bp
ATGGAGCCCGGCCCCGACGGCCCCGCCGCCTCCGGCCCCGCCGCCATCCGCGAGGGCTGG
TTCCGCGAGACCTGCAGCCTGTGGCCCGGCCAGGCCCTGTCACTGCAGGTGGAGCAGCTG
CTCCACCACCGGCGCTCGCGCTACCAGGACATCCTCGTCTTCCGCAGTAAGACCTATGGC
AACGTGCTGGTGTTGGACGGTGTCATCCAGTGCACGGAGAGAGACGAGTTCTCCTACCAG
GAGATGATCGCCAACCTGCCTCTCTGCAGCCACCCCAACCCGCGAAAGGTGCTGATCATC
GGGGGCGGAGATGGAGGTGTCCTGCGGGAGGTGGTGAAGCACCCCTCCGTGGAGTCCGTG
GTCCAGTGTGAGATCGACGAGGATGTCATCCAAGTCTCCAAGAAGTTCCTGCCAGGCATG
GCCATTGGCTACTCTAGCTCGAAGCTGACCCTACATGTGGGTGACGGTTTTGAGTTCATG
AAACAGAATCAGGATGCCTTCGACGTGATCATCACTGACTCCTCAGACCCCATGGGCCCC
GCCGAAAGTCTCTTCAAGGAGTCCTATTACCAGCTCATGAAGACAGCCCTCAAGGAAGAT
GGTGTCCTCTGCTGCCAGGGCGAGTGCCAGTGGCTGCACCTGGACCTCATCAAGGAGATG
CGGCAGTTCTGCCAGTCCCTGTTCCCCGTGGTGGCCTATGCCTACTGCACCATCCCCACC
TACCCCAGCGGCCAGATCGGCTTCATGCTGTGCAGCAAGAACCCGAGCACGAACTTCCAG
GAGCCGGTGCAGCCGCTGACACAGCAGCAGGTGGCGCAGATGCAGCTGAAGTACTACAAC
TCCGACGTGCACCGCGCCGCCTTTGTGCTGCCCGAGTTTGCCCGCAAGGCCCTGAATGAT
GTGAGCTGA
Enzyme 2 GenBank Gene ID AL109811 Link Image
Enzyme 2 GeneCard ID SRM Link Image
Enzyme 2 GenAtlas ID SRM Link Image
Enzyme 2 HGNC ID HGNC:11296 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p36-p22
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Wahlfors J, Alhonen L, Kauppinen L, Hyvonen T, Janne J, Eloranta TO: Human spermidine synthase: cloning and primary structure. DNA Cell Biol. 1990 Mar;9(2):103-10. [PubMed Link Image]
  2. Myohanen S, Kauppinen L, Wahlfors J, Alhonen L, Janne J: Human spermidine synthase gene: structure and chromosomal localization. DNA Cell Biol. 1991 Jul-Aug;10(6):467-74. [PubMed Link Image]
  3. 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]
  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. 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]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 13000
Enzyme 3 Name Spermidine synthase (Spermidine synthase, isoform CRA_a)
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name SRM
Enzyme 3 Protein Sequence >Spermidine synthase (Spermidine synthase, isoform CRA_a)
MEPGPDGPAASGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYG
NVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESV
VQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGP
AESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFPVVAYAYCTIPT
YPSGQIGFMLCSKNPSTNFQEPVQPLTQQQVAQMQLKYYNSDVHRAAFVLPEFARKALND
VS
Enzyme 3 Number of Residues 302
Enzyme 3 Molecular Weight 33825
Enzyme 3 Theoretical pI Not Available
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Not Available
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 Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID B1AKP9 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name B1AKP9_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 Not Available
Enzyme 3 GeneCard ID B1AKP9 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 13069
Enzyme 4 Name Adenosylmethionine decarboxylase 1
Enzyme 4 Synonyms
  1. SubName: Adenosylmethionine decarboxylase 1, isoform CRA_b
  2. SubName: Putative uncharacterized protein DKFZp313L1234
Enzyme 4 Gene Name AMD1
Enzyme 4 Protein Sequence >Adenosylmethionine decarboxylase 1
MGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESG
IRDLIPGSVIDATMFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLI
RKVVEVFKPGKFVTTLFVNQSSKCRTVLASPQKIEGFKRLDCQSAMFNDYNFVFTSFAKK
QQQQQS
Enzyme 4 Number of Residues 186
Enzyme 4 Molecular Weight 21301.0
Enzyme 4 Theoretical pI 4.67
Enzyme 4 GO Classification
Function
  • adenosylmethionine decarboxylase activity
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • metabolic process
  • polyamine biosynthetic process
  • polyamine metabolic process
  • spermidine biosynthetic process
  • spermine biosynthetic process
Component
Enzyme 4 General Function Involved in adenosylmethionine decarboxylase 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 55664719 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q5VXN4 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name Q5VXN4_HUMAN Link Image
Enzyme 4 PDB ID 1MSV Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >561 bp
ATGGGACGTATGAATTCTGACTGTTGGTACTTATATACTCTGGATTTCCCAGAGAGTCGG
GTAATCAGTCAGCCAGATCAAACCTTGGAAATTCTGATGAGTGAGCTTGACCCAGCAGTT
ATGGACCAGTTCTACATGAAAGATGGTGTTACTGCAAAGGATGTCACTCGTGAGAGTGGA
ATTCGTGACCTGATACCAGGTTCTGTCATTGATGCCACAATGTTCAATCCTTGTGGGTAT
TCGATGAATGGAATGAAATCGGATGGAACTTATTGGACTATTCACATCACTCCAGAACCA
GAATTTTCTTATGTTAGCTTTGAAACAAACTTAAGTCAGACCTCCTATGATGACCTGATC
AGGAAAGTTGTAGAAGTCTTCAAGCCAGGAAAATTTGTGACCACCTTGTTTGTTAATCAG
AGTTCTAAATGTCGCACAGTGCTTGCTTCGCCCCAGAAGATTGAAGGTTTTAAGCGTCTT
GATTGCCAGAGTGCTATGTTCAATGATTACAATTTTGTTTTTACCAGTTTTGCTAAGAAG
CAGCAACAACAGCAGAGTTGA
Enzyme 4 GenBank Gene ID AL357515 Link Image
Enzyme 4 GeneCard ID AMD1 Link Image
Enzyme 4 GenAtlas ID AMD1 Link Image
Enzyme 4 HGNC ID HGNC:457 Link Image
Enzyme 4 Chromosome Location 6
Enzyme 4 Locus 6q21
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available