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EC
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1.13.11.42
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| Deleted entry: | indoleamine-pyrrole 2,3-dioxygenase. The enzyme was identical to EC 1.13.11.11, tryptophan 2,3-dioxygenase |
| [EC 1.13.11.42 created 1992, deleted 2006] |
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| EC |
1.14.16.4 |
| Accepted name: |
tryptophan 5-monooxygenase |
| Reaction: |
L-tryptophan + a 5,6,7,8-tetrahydropteridine + O2 = 5-hydroxy-L-tryptophan + a 4a-hydroxy-5,6,7,8-tetrahydropteridine |
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For diagram of biopterin biosynthesis, click here |
| Other name(s): |
L-tryptophan hydroxylase; indoleacetic acid-5-hydroxylase; tryptophan 5-hydroxylase; tryptophan hydroxylase |
| Systematic name: |
L-tryptophan,tetrahydropteridine:oxygen oxidoreductase (5-hydroxylating) |
| Comments: |
The active centre contains mononuclear iron(II). The enzyme is activated by phosphorylation, catalysed by a Ca2+-activated protein kinase. The 4a-hydroxytetrahydropteridine formed can dehydrate to 6,7-dihydropteridine, both spontaneously and by the action of EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase. The 6,7-dihydropteridine must be enzymically reduced back to tetrahydropteridine, by EC 1.5.1.34, 6,7-dihydropteridine reductase, before it slowly rearranges into the more stable but inactive compound 7,8-dihydropteridine. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9037-21-2 |
| References: |
| 1. |
Friedman, P.A., Kappelman, A.H. and Kaufman, S. Partial purification and characterization of tryptophan hydroxylase from rabbit hindbrain. J. Biol. Chem. 247 (1972) 4165–4173. [PMID: 4402511] |
| 2. |
Hamon, M., Bourgoin, S., Artaud, F. and Glowinski, J. The role of intraneuronal 5-HT and of tryptophan hydroxylase activation in the control of 5-HT synthesis in rat brain slices incubated in K+-enriched medium. J. Neurochem. 33 (1979) 1031–1042. [DOI] [PMID: 315449] |
| 3. |
Ichiyama, A., Nakamura, S., Nishizuka, Y. and Hayaishi, O. Enzymic studies on the biosynthesis of serotonin in mammalian brain. J. Biol. Chem. 245 (1970) 1699–1709. [PMID: 5309585] |
| 4. |
Jequier, E., Robinson, B.S., Lovenberg, W. and Sjoerdsma, A. Further studies on tryptophan hydroxylase in rat brainstem and beef pineal. Biochem. Pharmacol. 18 (1969) 1071–1081. [DOI] [PMID: 5789774] |
| 5. |
Wang, L., Erlandsen, H., Haavik, J., Knappskog, P.M. and Stevens, R.C. Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin. Biochemistry 41 (2002) 12569–12574. [DOI] [PMID: 12379098] |
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| [EC 1.14.16.4 created 1972, modified 2003, modified 2019] |
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| EC |
2.1.1.4 |
| Accepted name: |
acetylserotonin O-methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin |
| Glossary: |
melatonin = N-acetyl-5-methoxytryptamine
serotonin = 5-hydroxytryptamine
tryptamine = 2-(1H-indol-3-yl)ethanamine |
| Other name(s): |
hydroxyindole methyltransferase; hydroxyindole O-methyltransferase; N-acetylserotonin O-methyltransferase; acetylserotonin methyltransferase |
| Systematic name: |
S-adenosyl-L-methionine:N-acetylserotonin O-methyltransferase |
| Comments: |
Some other hydroxyindoles also act as acceptor, but more slowly. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-77-0 |
| References: |
| 1. |
Axelrod, J. and Weissbach, H. Purification and properties of hydroxyindole-O-methyl transferase. J. Biol. Chem. 236 (1961) 211–213. [PMID: 13685335] |
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| [EC 2.1.1.4 created 1961] |
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| EC |
2.3.1.87 |
| Accepted name: |
aralkylamine N-acetyltransferase |
| Reaction: |
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine |
| Other name(s): |
serotonin acetyltransferase; serotonin acetylase; arylalkylamine N-acetyltransferase; serotonin N-acetyltransferase; AANAT; melatonin rhythm enzyme |
| Systematic name: |
acetyl-CoA:2-arylethylamine N-acetyltransferase |
| Comments: |
Narrow specificity towards 2-arylethylamines, including serotonin (5-hydroxytryptamine), tryptamine, 5-methoxytryptamine and phenylethylamine. This is the penultimate enzyme in the production of melatonin (5-methoxy-N-acetyltryptamine) and controls its synthesis (cf. EC 2.1.1.4, acetylserotonin O-methyltransferase). Differs from EC 2.3.1.5 arylamine N-acetyltransferase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 92941-56-5 |
| References: |
| 1. |
Voisin, P., Namboodiri, M.A.A. and Klein, D.C. Arylamine N-acetyltransferase and arylalkylamine N-acetyltransferase in the mammalian pineal gland. J. Biol. Chem. 259 (1984) 10913–10918. [PMID: 6469990] |
| 2. |
Ferry, G., Loynel, A., Kucharczyk, N., Bertin, S., Rodriguez, M., Delagrange, P., Galizzi, J.P., Jacoby, E., Volland, J.P., Lesieur, D., Renard, P., Canet, E., Fauchere, J.L. and Boutin, J.A. Substrate specificity and inhibition studies of human serotonin N-acetyltransferase. J. Biol. Chem. 275 (2000) 8794–8805. [DOI] [PMID: 10722724] |
| 3. |
Khalil, E.M. and Cole, P.A. A potent inhibitor of the melatonin rhythm enzyme. J. Am. Chem. Soc. 120 (1998) 6195–6196. |
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| [EC 2.3.1.87 created 1986, modified 2005] |
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| EC |
3.5.1.76 |
| Accepted name: |
arylalkyl acylamidase |
| Reaction: |
N-acetylarylalkylamine + H2O = arylalkylamine + acetate |
| Other name(s): |
aralkyl acylamidase |
| Systematic name: |
N-acetylarylalkylamine amidohydrolase |
| Comments: |
Identified in Pseudomonas putida. Strict specificity for N-acetyl arylalkylamines, including N-acetyl-2-phenylethylamine, N-acetyl-3-phenylpropylamine, N-acetyldopamine, N-acetyl-serotonin and melatonin. It also accepts arylalkyl acetates but not acetanilide derivatives, which are common substrates of EC 3.5.1.13, aryl acylamidase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Shimizu, S., Ogawa, J., Chung, M.C.-M., Yamada, H. Purification and characterization of a novel enzyme, arylalkyl acylamidase, from Pseudomonas putida Sc2. Eur. J. Biochem. 209 (1992) 375–382. [DOI] [PMID: 1396711] |
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| [EC 3.5.1.76 created 1999] |
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