EC |
1.4.3.4 |
Accepted name: |
monoamine oxidase |
Reaction: |
RCH2NHR′ + H2O + O2 = RCHO + R′NH2 + H2O2 |
Other name(s): |
adrenalin oxidase; adrenaline oxidase; amine oxidase (ambiguous); amine oxidase (flavin-containing); amine:oxygen oxidoreductase (deaminating) (flavin-containing); epinephrine oxidase; MAO; MAO A; MAO B; MAO-A; MAO-B; monoamine oxidase A; monoamine oxidase B; monoamine:O2 oxidoreductase (deaminating); polyamine oxidase (ambiguous); serotonin deaminase; spermidine oxidase (ambiguous); spermine oxidase (ambiguous); tyraminase; tyramine oxidase |
Systematic name: |
amine:oxygen oxidoreductase (deaminating) |
Comments: |
A mitochondrial outer-membrane flavoprotein (FAD) that catalyses the oxidative deamination of neurotransmitters and biogenic amines [3]. Acts on primary amines, and also on some secondary and tertiary amines. It differs from EC 1.4.3.21, primary-amine oxidase as it can oxidize secondary and tertiary amines but not methylamine. This enzyme is inhibited by acetylenic compounds such as chlorgyline, 1-deprenyl and pargyline but, unlike EC 1.4.3.21 and EC 1.4.3.22 (diamine oxidase), it is not inhibited by semicarbazide. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-66-5 |
References: |
1. |
Blaschko, H. Amine oxidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 337–351. |
2. |
Dostert, P.L., Strolin Benedetti, M. and Tipton, K.F. Interactions of monoamine oxidase with substrates and inhibitors. Med. Res. Rev. 9 (1989) 45–89. [DOI] [PMID: 2644497] |
3. |
Edmondson, D.E., Mattevi, A., Binda, C., Li, M. and Hubálek, F. Structure and mechanism of monoamine oxidase. Curr. Med. Chem. 11 (2004) 1983–1993. [PMID: 15279562] |
4. |
Shih, J.C. and Chen, K. Regulation of MAO-A and MAO-B gene expression. Curr. Med. Chem. 11 (2004) 1995–2005. [PMID: 15279563] |
5. |
Tipton, K.F., Boyce, S., O'Sullivan, J., Davey, G.P. and Healy, J. Monoamine oxidases: certainties and uncertainties. Curr. Med. Chem. 11 (2004) 1965–1982. [PMID: 15279561] |
6. |
De Colibus, L., Li, M., Binda, C., Lustig, A., Edmondson, D.E. and Mattevi, A. Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. Proc. Natl. Acad. Sci. USA 102 (2005) 12684–12689. [DOI] [PMID: 16129825] |
7. |
Youdim, M.B., Edmondson, D. and Tipton, K.F. The therapeutic potential of monoamine oxidase inhibitors. Nat. Rev. Neurosci. 7 (2006) 295–309. [DOI] [PMID: 16552415] |
8. |
Youdim, M.B. and Bakhle, Y.S. Monoamine oxidase: isoforms and inhibitors in Parkinson′s disease and depressive illness. Br. J. Pharmacol. 147 Suppl. 1 (2006) S287–S296. [DOI] [PMID: 16402116] |
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[EC 1.4.3.4 created 1961, modified 1983 (EC 1.4.3.9 created 1972, incorporated 1984), modified 2008] |
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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 |
2.3.1.5 |
Accepted name: |
arylamine N-acetyltransferase |
Reaction: |
acetyl-CoA + an arylamine = CoA + an N-acetylarylamine |
Other name(s): |
arylamine acetylase; β-naphthylamine N-acetyltransferase; 4-aminobiphenyl N-acetyltransferase; acetyl CoA-arylamine N-acetyltransferase; 2-naphthylamine N-acetyltransferase; arylamine acetyltransferase; indoleamine N-acetyltransferase; N-acetyltransferase (ambiguous); p-aminosalicylate N-acetyltransferase; serotonin acetyltransferase; serotonin N-acetyltransferase |
Systematic name: |
acetyl-CoA:arylamine N-acetyltransferase |
Comments: |
Wide specificity for aromatic amines, including serotonin; also catalyses acetyl-transfer between arylamines without CoA. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-33-2 |
References: |
1. |
Chou, T.C. and Lipmann, F. Separation of acetyl transfer enzymes in pigeon liver extract. J. Biol. Chem. 196 (1952) 89–103. [PMID: 12980945] |
2. |
Paul, R.C. and Ratledge, C. Further studies on anthranilate N-acetylanthranilic acid in Aerobacter aerogenes. Biochim. Biophys. Acta 320 (1973) 9–15. [DOI] [PMID: 4748369] |
3. |
Tabor, H., Mehler, A.H. and Stadtman, E.R. The enzymatic acetylation of amines. J. Biol. Chem. 204 (1953) 127–138. [PMID: 13084583] |
4. |
Weissbach, H., Redfield, B.G. and Axelrod, J. The enzymic acetylation of serotonin and other naturally occurring amines. Biochim. Biophys. Acta 54 (1961) 190–192. [DOI] [PMID: 14005907] |
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[EC 2.3.1.5 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
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2.7.1.123
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Transferred entry: | Ca2+/calmodulin-dependent protein kinase. Now EC 2.7.11.17, Ca2+/calmodulin-dependent protein kinase
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[EC 2.7.1.123 created 1989, deleted 2005] |
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EC |
2.7.11.17 |
Accepted name: |
Ca2+/calmodulin-dependent protein kinase |
Reaction: |
ATP + a protein = ADP + a phosphoprotein |
Other name(s): |
ATP:caldesmon O-phosphotransferase; caldesmon kinase; caldesmon kinase (phosphorylating); Ca2+/calmodulin-dependent microtubule-associated protein 2 kinase; Ca2+/calmodulin-dependent protein kinase 1; Ca2+/calmodulin-dependent protein kinase II; Ca2+/calmodulin-dependent protein kinase IV; Ca2+/calmodulin-dependent protein kinase kinase; Ca2+/calmodulin-dependent protein kinase kinase β; calmodulin-dependent kinase II; CaM kinase; CaM kinase II; CAM PKII; CaM-regulated serine/threonine kinase; CaMKI; CaMKII; CaMKIV; CaMKKα; CaMKKβ; microtubule-associated protein 2 kinase; STK20 |
Systematic name: |
ATP:protein phosphotransferase (Ca2+/calmodulin-dependent) |
Comments: |
Requires calmodulin and Ca2+ for activity. A wide range of proteins can act as acceptor, including vimentin, synapsin, glycogen synthase, myosin light chains and the microtubule-associated tau protein. Not identical with EC 2.7.11.18 (myosin-light-chain kinase) or EC 2.7.11.26 (tau-protein kinase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 141467-21-2 |
References: |
1. |
Adlersberg, M., Liu, K.P., Hsiung, S.C., Ehrlich, Y. and Tamir, H. A Ca2+-dependent protein kinase activity associated with serotonin binding protein. J. Neurochem. 49 (1987) 1105–1115. [DOI] [PMID: 3040904] |
2. |
Baudier, J. and Cole, R.D. Phosphorylation of tau proteins to a state like that in Alzheimer's brain is catalyzed by a calcium/calmodulin-dependent kinase and modulated by phospholipids. J. Biol. Chem. 262 (1987) 17577–17583. [PMID: 3121601] |
3. |
Schulman, H., Kuret, J., Jefferson, A.B., Nose, P.S. and Spitzer, K.H. Ca2+/calmodulin-dependent microtubule-associated protein 2 kinase: broad substrate specificity and multifunctional potential in diverse tissues. Biochemistry 24 (1985) 5320–5327. [PMID: 4074698] |
4. |
Anderson, K.A., Means, R.L., Huang, Q.H., Kemp, B.E., Goldstein, E.G., Selbert, M.A., Edelman, A.M., Fremeau, R.T. and Means, A.R. Components of a calmodulin-dependent protein kinase cascade. Molecular cloning, functional characterization and cellular localization of Ca2+/calmodulin-dependent protein kinase kinase beta. J. Biol. Chem. 273 (1998) 31880–31889. [DOI] [PMID: 9822657] |
5. |
Matsushita, M. and Nairn, A.C. Characterization of the mechanism of regulation of Ca2+/ calmodulin-dependent protein kinase I by calmodulin and by Ca2+/calmodulin-dependent protein kinase kinase. J. Biol. Chem. 273 (1998) 21473–21481. [DOI] [PMID: 9705275] |
6. |
Ohmstede, C.A., Jensen, K.F. and Sahyoun, N.E. Ca2+/calmodulin-dependent protein kinase enriched in cerebellar granule cells. Identification of a novel neuronal calmodulin-dependent protein kinase. J. Biol. Chem. 264 (1989) 5866–5875. [PMID: 2538431] |
7. |
Rieker, J.P., Swanljung-Collins, H. and Collins, J.H. Purification and characterization of a calmodulin-dependent myosin heavy chain kinase from intestinal brush border. J. Biol. Chem. 262 (1987) 15262–15268. [PMID: 2822719] |
8. |
Iwasa, T., Inoue, N., Fukunaga, K., Isobe, T., Okuyama, T. and Miyamoto, E. Purification and characterization of a multifunctional calmodulin-dependent protein kinase from canine myocardial cytosol. Arch. Biochem. Biophys. 248 (1986) 21–29. [DOI] [PMID: 3089163] |
9. |
Gomes, A.V., Barnes, J.A. and Vogel, H.J. Spectroscopic characterization of the interaction between calmodulin-dependent protein kinase I and calmodulin. Arch. Biochem. Biophys. 379 (2000) 28–36. [DOI] [PMID: 10864438] |
10. |
Mal, T.K., Skrynnikov, N.R., Yap, K.L., Kay, L.E. and Ikura, M. Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR. Biochemistry 41 (2002) 12899–12906. [DOI] [PMID: 12390014] |
11. |
Ngai, P.K. and Walsh, M.P. Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase activity by caldesmon. J. Biol. Chem. 259 (1984) 13656–13659. [PMID: 6150036] |
12. |
Ikebe, M., Reardon, S., Scott-Woo, G.C., Zhou, Z. and Koda, Y. Purification and characterization of calmodulin-dependent multifunctional protein kinase from smooth muscle: isolation of caldesmon kinase. Biochemistry 29 (1990) 11242–11248. [PMID: 2176896] |
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[EC 2.7.11.17 created 1989 as EC 2.7.1.123, transferred 2005 to EC 2.7.11.17 (EC 2.7.1.120 incorporated 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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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 |
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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] |
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[EC 4.1.1.28 created 1961 (EC 4.1.1.26 and EC 4.1.1.27 both created 1961 and incorporated 1972)] |
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