The Enzyme Database

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EC 1.13.11.11     
Accepted name: tryptophan 2,3-dioxygenase
Reaction: L-tryptophan + O2 = N-formyl-L-kynurenine
For diagram of tryptophan catabolism, click here
Other name(s): tryptophan pyrrolase (ambiguous); tryptophanase; tryptophan oxygenase; tryptamine 2,3-dioxygenase; tryptophan peroxidase; indoleamine 2,3-dioxygenase (ambiguous); indolamine 2,3-dioxygenase (ambiguous); L-tryptophan pyrrolase; TDO; L-tryptophan 2,3-dioxygenase; L-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: L-tryptophan:oxygen 2,3-oxidoreductase (ring-opening)
Comments: A protohemoprotein. In mammals, the enzyme appears to be located only in the liver. This enzyme, together with EC 1.13.11.52, indoleamine 2,3-dioxygenase, catalyses the first and rate-limiting step in the kynurenine pathway, the major pathway of tryptophan metabolism [5]. The enzyme is specific for tryptophan as substrate, but is far more active with L-tryptophan than with D-tryptophan [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9014-51-1
References:
1.  Uchida, K., Shimizu, T., Makino, R., Sakaguchi, K., Iizuka, T., Ishimura, Y., Nozawa, T. and Hatano, M. Magnetic and natural circular dichroism of L-tryptophan 2,3-dioxygenases and indoleamine 2,3-dioxygenase. I. Spectra of ferric and ferrous high spin forms. J. Biol. Chem. 258 (1983) 2519–2525. [PMID: 6600455]
2.  Ren, S., Liu, H., Licad, E. and Correia, M.A. Expression of rat liver tryptophan 2,3-dioxygenase in Escherichia coli: structural and functional characterization of the purified enzyme. Arch. Biochem. Biophys. 333 (1996) 96–102. [DOI] [PMID: 8806758]
3.  Leeds, J.M., Brown, P.J., McGeehan, G.M., Brown, F.K. and Wiseman, J.S. Isotope effects and alternative substrate reactivities for tryptophan 2,3-dioxygenase. J. Biol. Chem. 268 (1993) 17781–17786. [PMID: 8349662]
4.  Dang, Y., Dale, W.E. and Brown, O.R. Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway. Free Radic. Biol. Med. 28 (2000) 615–624. [DOI] [PMID: 10719243]
5.  Littlejohn, T.K., Takikawa, O., Truscott, R.J. and Walker, M.J. Asp274 and His346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase. J. Biol. Chem. 278 (2003) 29525–29531. [DOI] [PMID: 12766158]
[EC 1.13.11.11 created 1961 as EC 1.11.1.4, deleted 1964, reinstated 1965 as EC 1.13.1.12, transferred 1972 to EC 1.13.11.11, modified 1989, modified 2006]
 
 
EC 1.14.99.59     
Accepted name: tryptamine 4-monooxygenase
Reaction: tryptamine + reduced acceptor + O2 = 4-hydroxytryptamine + acceptor + H2O
For diagram of psilocybin biosynthesis, click here
Glossary: psilocybin = 3-[2-(dimethylamino)ethyl]-1H-indol-4-yl phosphate
Other name(s): PsiH
Systematic name: tryptamine,hydrogen-donor:oxygen oxidoreductase (4-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the fungus Psilocybe cubensis. Involved in the biosynthesis of the psychoactive compound psilocybin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Fricke, J., Blei, F. and Hoffmeister, D. Enzymatic synthesis of psilocybin. Angew. Chem. Int. Ed. Engl. 56 (2017) 12352–12355. [DOI] [PMID: 28763571]
[EC 1.14.99.59 created 2017]
 
 
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, 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]
[EC 2.1.1.4 created 1961]
 
 
EC 2.1.1.49     
Accepted name: amine N-methyltransferase
Reaction: S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine
Other name(s): nicotine N-methyltransferase; tryptamine N-methyltransferase; arylamine N-methyltransferase; tryptamine methyltransferase
Systematic name: S-adenosyl-L-methionine:amine N-methyltransferase
Comments: An enzyme of very broad specificity; many primary, secondary and tertiary amines can act as acceptors, including tryptamine, aniline, nicotine and a variety of drugs and other xenobiotics.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 51377-47-0, 111694-10-1
References:
1.  Ansher, S.S. and Jakoby, W.B. Amine N-methyltransferases from rabbit liver. J. Biol. Chem. 261 (1986) 3996–4001. [PMID: 3949799]
2.  Crooks, P.A., Godin, C.S., Damani, L.A., Ansher, S.S. and Jakoby, W.B. Formation of quaternary amines by N-methylation of azaheterocycles with homogeneous amine N-methyltransferases. Biochem. Pharmacol. 37 (1988) 1673–1677. [DOI] [PMID: 3377829]
[EC 2.1.1.49 created 1976, modified 1990 (EC 2.1.1.81 created 1989, incorporated 1990)]
 
 
EC 2.1.1.345     
Accepted name: psilocybin synthase
Reaction: 2 S-adenosyl-L-methionine + 4-hydroxytryptamine 4-phosphate = 2 S-adenosyl-L-homocysteine + psilocybin (overall reaction)
(1a) S-adenosyl-L-methionine + 4-hydroxytryptamine 4-phosphate = S-adenosyl-L-homocysteine + 4-hydroxy-N-methyltryptamine 4-phosphate
(1b) S-adenosyl-L-methionine + 4-hydroxy-N-methyltryptamine 4-phosphate = S-adenosyl-L-homocysteine + psilocybin
For diagram of psilocybin biosynthesis, click here
Glossary: psilocybin = 3-[2-(dimethylamino)ethyl]-1H-indol-4-yl phosphate
Other name(s): PsiM
Systematic name: S-adenosyl-L-methionine:4-hydroxytryptamine-4-phosphate N,N-dimethyltransferase
Comments: Isolated from the fungus Psilocybe cubensis. The product, psilocybin, is a psychoactive compound.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Fricke, J., Blei, F. and Hoffmeister, D. Enzymatic synthesis of psilocybin. Angew. Chem. Int. Ed. Engl. 56 (2017) 12352–12355. [DOI] [PMID: 28763571]
[EC 2.1.1.345 created 2017]
 
 
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.
[EC 2.3.1.87 created 1986, modified 2005]
 
 
EC 2.7.1.222     
Accepted name: 4-hydroxytryptamine kinase
Reaction: ATP + 4-hydroxytryptamine = ADP + 4-hydroxytryptamine 4-phosphate
For diagram of psilocybin biosynthesis, click here
Glossary: psilocybin = 3-[2-(dimethylamino)ethyl]-1H-indol-4-yl phosphate
Other name(s): PsiK
Systematic name: ATP:4-hydroxytryptamine 4-phosphotransferase
Comments: Also acts on 4-hydroxy-L-tryptophan in vitro. Isolated from the fungus Psilocybe cubensis. Involved in the biosynthesis of the psychoactive compound psilocybin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Fricke, J., Blei, F. and Hoffmeister, D. Enzymatic synthesis of psilocybin. Angew. Chem. Int. Ed. Engl. 56 (2017) 12352–12355. [DOI] [PMID: 28763571]
[EC 2.7.1.222 created 2017]
 
 
EC 4.1.1.28     
Accepted name: aromatic-L-amino-acid decarboxylase
Reaction: (1) L-dopa = dopamine + CO2
(2) 5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2
For diagram of dopa biosynthesis, click here and for diagram of indole and ipecac alkaloid biosynthesis, click here
Glossary: dopamine = 4-(2-aminoethyl)benzene-1,2-diol
L-dopa = 3,4-dihydroxyphenylalanine
Other name(s): DOPA decarboxylase; tryptophan decarboxylase; hydroxytryptophan decarboxylase; L-DOPA decarboxylase; aromatic amino acid decarboxylase; 5-hydroxytryptophan decarboxylase; aromatic-L-amino-acid carboxy-lyase (tryptamine-forming)
Systematic name: aromatic-L-amino-acid carboxy-lyase
Comments: A pyridoxal-phosphate protein. The enzyme also acts on some other aromatic L-amino acids, including L-tryptophan, L-tyrosine and L-phenylalanine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9042-64-2
References:
1.  Christenson, J.G., Dairman, W. and Udenfriend, S. On the identity of DOPA decarboxylase and 5-hydroxytryptophan decarboxylase (immunological titration-aromatic L-amino acid decarboxylase-serotonin-dopamine-norepinephrine). Proc. Natl. Acad. Sci. USA 69 (1972) 343–347. [DOI] [PMID: 4536745]
2.  Lovenberg, W., Weissbach, H. and Udenfriend, S. Aromatic L-amino acid decarboxylase. J. Biol. Chem. 237 (1962) 89–93. [PMID: 14466899]
3.  McGilvery, R.W. and Cohen, P.P. The decarboxylation of L-phenylalanine by Streptococcus faecalis R. J. Biol. Chem. 174 (1948) 813–816. [PMID: 18871240]
4.  Sekeris, C.E. Zur Tyrosinstoffwechsel der Insekten. XII. Reinigung, Eigenschaften und Substratspezifität der DOPA-Decarboxylase. Hoppe-Seyler's Z. Physiol. Chem. 332 (1963) 70–78. [PMID: 14054806]
5.  Weissbach, H., Bogdanski, D.F., Redfield, B.G. and Udenfriend, S. Studies on the effect of vitamin B6 on 5-hydroxytryptamine (serotonin) formation. J. Biol. Chem. 227 (1957) 617–624. [PMID: 13462983]
[EC 4.1.1.28 created 1961 (EC 4.1.1.26 and EC 4.1.1.27 both created 1961 and incorporated 1972)]
 
 
EC 4.1.1.105     
Accepted name: L-tryptophan decarboxylase
Reaction: L-tryptophan = tryptamine + CO2
For diagram of psilocybin biosynthesis, click here
Other name(s): psiD (gene name); TDC (gene name)
Systematic name: L-tryptophan carboxy-lyase
Comments: The enzyme has been characterized from bacteria, plants, and fungi. Unlike EC 4.1.1.28, aromatic-L-amino-acid decarboxylase, this enzyme is specific for L-tryptophan.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Noe, W., Mollenschott, C. and Berlin, J. Tryptophan decarboxylase from Catharanthus roseus cell suspension cultures: purification, molecular and kinetic data of the homogenous protein. Plant Mol. Biol. 3 (1984) 281–288. [DOI] [PMID: 24310513]
2.  Buki, K.G., Vinh, D.Q. and Horvath, I. Partial purification and some properties of tryptophan decarboxylase from a Bacillus strain. Acta Microbiol Hung 32 (1985) 65–73. [PMID: 4036551]
3.  Nakazawa, H., Kumagai, H. and Yamada, H. Constitutive aromatic L-amino acid decarboxylase from Micrococcus percitreus. Biochem. Biophys. Res. Commun. 61 (1974) 75–82. [DOI] [PMID: 4441405]
4.  Lopez-Meyer, M. and Nessler, C.L. Tryptophan decarboxylase is encoded by two autonomously regulated genes in Camptotheca acuminata which are differentially expressed during development and stress. Plant J. 11 (1997) 1167–1175. [DOI] [PMID: 9225462]
5.  Fricke, J., Blei, F. and Hoffmeister, D. Enzymatic synthesis of psilocybin. Angew. Chem. Int. Ed. Engl. 56 (2017) 12352–12355. [DOI] [PMID: 28763571]
[EC 4.1.1.105 created 2017]
 
 
EC 4.3.3.2     
Accepted name: strictosidine synthase
Reaction: 3-α(S)-strictosidine + H2O = tryptamine + secologanin
For diagram of indole and ipecac alkaloid biosynthesis, click here
Other name(s): strictosidine synthetase; STR; 3-α(S)-strictosidine tryptamine-lyase
Systematic name: 3-α(S)-strictosidine tryptamine-lyase (secologanin-forming)
Comments: Catalyses a Pictet-Spengler reaction between the aldehyde group of secologanin and the amino group of tryptamine [4,5]. Involved in the biosynthesis of the monoterpenoid indole alkaloids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 69669-72-3
References:
1.  Treimer, J.K. and Zenk, M.H. Purification and properties of strictosidine synthase, the key enzyme in indole alkaloid formation. Eur. J. Biochem. 101 (1979) 225–233. [DOI] [PMID: 510306]
2.  Kutchan, T.M. Strictosidine: from alkaloid to enzyme to gene. Phytochemistry 32 (1993) 493–506. [DOI] [PMID: 7763429]
3.  de Waal, A., Meijer, A.H. and Verpoorte, R. Strictosidine synthase from Catharanthus roseus: purification and characterization of multiple forms. Biochem. J. 306 (1995) 571–580. [PMID: 7887913]
4.  Ruppert, M., Woll, J., Giritch, A., Genady, E., Ma, X. and Stöckigt, J. Functional expression of an ajmaline pathway-specific esterase from Rauvolfia in a novel plant-virus expression system. Planta 222 (2005) 888–898. [DOI] [PMID: 16133216]
5.  McCoy, E., Galan, M.C. and O'Connor, S.E. Substrate specificity of strictosidine synthase. Bioorg. Med. Chem. Lett. 16 (2006) 2475–2478. [DOI] [PMID: 16481164]
6.  Ma, X., Panjikar, S., Koepke, J., Loris, E. and Stöckigt, J. The structure of Rauvolfia serpentina strictosidine synthase is a novel six-bladed β-propeller fold in plant proteins. Plant Cell 18 (2006) 907–920. [DOI] [PMID: 16531499]
[EC 4.3.3.2 created 1990]
 
 


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