Catecholamine synthesis (WP513)

Rattus norvegicus

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This pathway was created using information from: * http://biocyc.org/META/new-image?type=PATHWAY&object=PWY66-301 * http://www.chem.qmul.ac.uk/iubmb/enzyme/reaction/AminoAcid/dopa.html * http://www.chem.qmul.ac.uk/iubmb/enzyme/reaction/AminoAcid/PheTyr.html * http://www.genome.ad.jp/dbget-bin/www_bget?pathway+map00350 * http://www.genome.jp/dbget-bin/get_pathway?org_name=rno&mapno=00400 (phenylalanine -> tyrosine)

Authors

Anne Michielsen , Thomas Kelder , Noortje Van Der Vorst , Alex Pico , Kristina Hanspers , Christine Chichester , Egon Willighagen , and Lars Willighagen

Activity

last edited

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Cited In

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Organisms

Rattus norvegicus

Communities

Annotations

Pathway Ontology

catecholamine biosynthetic pathway

Participants

Label Type Compact URI Comment
L-DOPA Metabolite hmdb:HMDB0000609
Dopamine Metabolite hmdb:HMDB0000073
Adrenaline Metabolite hmdb:HMDB0000068
4a-hydroxy-tetrahydrobiopterin Metabolite pubchem.compound:23724532
Phenylalanine Metabolite hmdb:HMDB0000159
Ascorbate Metabolite hmdb:HMDB0000044
Noradrenaline Metabolite hmdb:HMDB0000216
L-tyrosine Metabolite hmdb:HMDB0000158
AdoHcy Metabolite hmdb:HMDB0000939
AdoMet Metabolite pubchem.compound:90473
tetrahydrobiopterin Metabolite hmdb:HMDB0000027
tetrahydrobiopterin Metabolite hmdb:HMDB0000027
Dehydroascorbate Metabolite hmdb:HMDB0001264
4a-hydroxy-tetrahydrobiopterin Metabolite pubchem.compound:23724532
Dbh GeneProduct ncbigene:25699
Pah GeneProduct ncbigene:24616
Th GeneProduct ncbigene:25085
Ddc GeneProduct ncbigene:24311
Pnmt GeneProduct ncbigene:24661

References

  1. On the identity of DOPA decarboxylase and 5-hydroxytryptophan decarboxylase (immunological titration-aromatic L-amino acid decarboxylase-serotonin-dopamine-norepinephrine). Christenson JG, Dairman W, Udenfriend S. Proc Natl Acad Sci U S A. 1972 Feb;69(2):343–7. PubMed Europe PMC Scholia
  2. Phenylalanine hydroxylation by Pseudomonas species (ATCC 11299a). Nature of the cofactor. Guroff G, Rhoads CA. J Biol Chem. 1969 Jan 10;244(1):142–6. PubMed Europe PMC Scholia
  3. 3,4-dihydroxyphenylethylamine beta-hydroxylase. Physical properties, copper content, and role of copper in the catalytic acttivity. Friedman S, Kaufman S. J Biol Chem. 1965 Dec;240(12):4763–73. PubMed Europe PMC Scholia
  4. Phenylalanine as substrate and inhibitor of tyrosine hydroxylase. Ikeda M, Levitt M, Udenfriend S. Arch Biochem Biophys. 1967 May;120(2):420–7. PubMed Europe PMC Scholia
  5. Tyrosine hydroxylase activation in depolarized dopaminergic terminals--involvement of Ca2+-dependent phosphorylation. El Mestikawy S, Glowinski J, Hamon M. Nature. 1983 Apr 28;302(5911):830–2. PubMed Europe PMC Scholia
  6. Mechanism of metal-independent hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase. Carr RT, Balasubramanian S, Hawkins PC, Benkovic SJ. Biochemistry. 1995 Jun 6;34(22):7525–32. PubMed Europe PMC Scholia
  7. Crystal structure of tyrosine hydroxylase at 2.3 A and its implications for inherited neurodegenerative diseases. Goodwill KE, Sabatier C, Marks C, Raag R, Fitzpatrick PF, Stevens RC. Nat Struct Biol. 1997 Jul;4(7):578–85. PubMed Europe PMC Scholia
  8. The chemical estimation of tyrosine and tyramine. UDENFRIEND S, COOPER JR. J Biol Chem. 1952 May;196(1):227–33. PubMed Europe PMC Scholia
  9. The enzymatic conversion of phenylalanine to tyrosine. KAUFMAN S. J Biol Chem. 1957 May;226(1):511–24. PubMed Europe PMC Scholia
  10. Studies on the effect of vitamin B6 on 5-hydroxytryptamine (serotonin) formation. WEISSBACH H, BOGDANSKI DF, REDFIELD BG, UDENFRIEND S. J Biol Chem. 1957 Aug;227(2):617–24. PubMed Europe PMC Scholia
  11. Studies on the enzyme catalyzing the conversion of 3,4-dihydroxyphenylethylamine to norepinephrine. LEVIN EY, KAUFMAN S. J Biol Chem. 1961 Jul;236:2043–9. PubMed Europe PMC Scholia
  12. Purification and properties of phenylethanolamine-N-methyl transferase. AXELROD J. J Biol Chem. 1962 May;237:1657–60. PubMed Europe PMC Scholia
  13. ON TYROSINE METABOLISM IN INSECTS. XII. PURIFICATION, PROPERTIES AND SUBSTRATE SPECIFICITY OF DOPA-DECARBOXYLASE. SEKERIS CE. Hoppe Seylers Z Physiol Chem. 1963;332:70–8. PubMed Europe PMC Scholia
  14. TYROSINE HYDROXYLASE. THE INITIAL STEP IN NOREPINEPHRINE BIOSYNTHESIS. NAGATSU T, LEVITT M, UDENFRIEND S. J Biol Chem. 1964 Sep;239:2910–7. PubMed Europe PMC Scholia
  15. Studies on the mechanism of the enzymatic conversion of phenylalanine to tyrosine. KAUFMAN S. J Biol Chem. 1959 Oct;234:2677–82. PubMed Europe PMC Scholia
  16. The enzymatic conversion of 3,4-dihydroxyphenylethylamine to norepinephrine. LEVIN EY, LEVENBERG B, KAUFMAN S. J Biol Chem. 1960 Jul;235:2080–6. PubMed Europe PMC Scholia
  17. Aromatic L-amino acid decarboxylase. LOVENBERG W, WEISSBACH H, UDENFRIEND S. J Biol Chem. 1962 Jan;237:89–93. PubMed Europe PMC Scholia
  18. The decarboxylation of L-phenylalanine by Streptococcus faecalis R. McGILVERY RW, COHEN PP. J Biol Chem. 1948 Jul;174(3):813–6. PubMed Europe PMC Scholia