The Enzyme Database

Your query returned 16 entries.    printer_iconPrintable version

EC 1.14.2.1      
Transferred entry: now EC 1.14.17.1, dopamine β-monooxygenase
[EC 1.14.2.1 created 1965, deleted 1972]
 
 
EC 1.14.13.8     
Accepted name: flavin-containing monooxygenase
Reaction: N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
Other name(s): dimethylaniline oxidase; dimethylaniline N-oxidase; FAD-containing monooxygenase; N,N-dimethylaniline monooxygenase; DMA oxidase; flavin mixed function oxidase; Ziegler’s enzyme; mixed-function amine oxidase; FMO; FMO-I; FMO-II; FMO1; FMO2; FMO3; FMO4; FMO5; flavin monooxygenase; methylphenyltetrahydropyridine N-monooxygenase; 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine:oxygen N-oxidoreductase; dimethylaniline monooxygenase (N-oxide-forming)
Systematic name: N,N-dimethylaniline,NADPH:oxygen oxidoreductase (N-oxide-forming)
Comments: A flavoprotein. A broad spectrum monooxygenase that accepts substrates as diverse as hydrazines, phosphines, boron-containing compounds, sulfides, selenides, iodide, as well as primary, secondary and tertiary amines [3,4]. This enzyme is distinct from other monooxygenases in that the enzyme forms a relatively stable hydroperoxy flavin intermediate [4,5]. This microsomal enzyme generally converts nucleophilic heteroatom-containing chemicals and drugs into harmless, readily excreted metabolites. For example, N-oxygenation is largely responsible for the detoxification of the dopaminergic neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) [2,6]
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-73-8
References:
1.  Ziegler, D.M. and Pettit, F.H. Microsomal oxidases. I. The isolation and dialkylarylamine oxygenase activity of pork liver microsomes. Biochemistry 5 (1966) 2932–2938. [PMID: 4381353]
2.  Chiba, K., Kubota, E., Miyakawa, T., Kato, Y. and Ishizaki, T. Characterization of hepatic microsomal metabolism as an in vivo detoxication pathway of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine in mice. J. Pharmacol. Exp. Ther. 246 (1988) 1108–1115. [PMID: 3262153]
3.  Cashman, J.R. Structural and catalytic properties of the mammalian flavin-containing monooxygenase. Chem. Res. Toxicol. 8 (1995) 165–181.
4.  Cashman, J.R. and Zhang, J. Human flavin-containing monooxygenases. Annu. Rev. Pharmacol. Toxicol. 46 (2006) 65–100. [DOI] [PMID: 16402899]
5.  Jones, K.C. and Ballou, D.P. Reactions of the 4a-hydroperoxide of liver microsomal flavin-containing monooxygenase with nucleophilic and electrophilic substrates. J. Biol. Chem. 261 (1986) 2553–2559. [PMID: 3949735]
6.  Chiba, K., Kobayashi, K., Itoh, K., Itoh, S., Chiba, T., Ishizaki, T. and Kamataki, T. N-Oxygenation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine by the rat liver flavin-containing monooxygenase expressed in yeast cells. Eur. J. Pharmacol. 293 (1995) 97–100. [PMID: 7672012]
[EC 1.14.13.8 created 1972 (EC 1.13.12.11 created 1992, part-incorporated 2006), modified 2006]
 
 
EC 1.14.16.2     
Accepted name: tyrosine 3-monooxygenase
Reaction: L-tyrosine + a 5,6,7,8-tetrahydropteridine + O2 = L-dopa + a 4a-hydroxy-5,6,7,8-tetrahydropteridine
For diagram of dopa biosynthesis, click here and for diagram of biopterin biosynthesis, click here
Glossary: L-dopa = 3,4-dihydroxy-L-phenylalanine
Other name(s): L-tyrosine hydroxylase; tyrosine 3-hydroxylase; tyrosine hydroxylase
Systematic name: L-tyrosine,tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating)
Comments: The active centre contains mononuclear iron(II). The enzyme is activated by phosphorylation, catalysed by EC 2.7.11.27, [acetyl-CoA carboxylase] 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: 9036-22-0
References:
1.  El Mestikawy, S., Glowinski, J. and Hamon, M. Tyrosine hydroxylase activation in depolarized dopaminergic terminals -involvement of Ca2+-dependent phosphorylation. Nature (Lond.) 302 (1983) 830–832. [PMID: 6133218]
2.  Ikeda, M., Levitt, M. and Udenfriend, S. Phenylalanine as substrate and inhibitor of tyrosine hydroxylase. Arch. Biochem. Biophys. 120 (1967) 420–427. [DOI] [PMID: 6033458]
3.  Nagatsu, T., Levitt, M. and Udenfriend, S. Tyrosine hydroxylase. The initial step in norepinephrine biosynthesis. J. Biol. Chem. 239 (1964) 2910–2917. [PMID: 14216443]
4.  Pigeon, D., Drissi-Daoudi, R., Gros, F. and Thibault, J. Copurification of tyrosine hydroxylase from rat pheochromocytoma by protein kinase. C. R. Acad. Sci. III 302 (1986) 435–438. [PMID: 2872947]
5.  Goodwill, K.E., Sabatier, C., Marks, C., Raag, R., Fitzpatrick, P.F. and Stevens, R.C. Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited neurodegenerative diseases. Nat. Struct. Biol. 4 (1997) 578–585. [PMID: 9228951]
[EC 1.14.16.2 created 1972, modified 2003, modified 2019]
 
 
EC 1.14.17.1     
Accepted name: dopamine β-monooxygenase
Reaction: dopamine + 2 ascorbate + O2 = noradrenaline + 2 monodehydroascorbate + H2O
For diagram of dopa biosynthesis, click here
Glossary: dopamine.html">dopamine = 4-(2-aminoethyl)benzene-1,2-diol
Other name(s): dopamine β-hydroxylase; MDBH (membrane-associated dopamine β-monooxygenase); SDBH (soluble dopamine β-monooxygenase); dopamine-B-hydroxylase; 3,4-dihydroxyphenethylamine β-oxidase; 4-(2-aminoethyl)pyrocatechol β-oxidase; dopa β-hydroxylase; dopamine β-oxidase; dopamine hydroxylase; phenylamine β-hydroxylase; (3,4-dihydroxyphenethylamine)β-mono-oxygenase; DβM (gene name)
Systematic name: dopamine,ascorbate:oxygen oxidoreductase (β-hydroxylating)
Comments: A copper protein. The enzyme, found in animals, binds two copper ions with distinct roles during catalysis. Stimulated by fumarate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-38-1
References:
1.  Levin, E.Y., Levenberg, B. and Kaufman, S. The enzymatic conversion of 3,4-dihydroxyphenylethylamine to norepinephrine. J. Biol. Chem. 235 (1960) 2080–2086. [PMID: 14416204]
2.  Friedman, S. and Kaufman, S. 3,4-Dihydroxyphenylethylamine β-hydroxylase. Physical properties, copper content, and role of copper in the catalytic activity. J. Biol. Chem. 240 (1965) 4763–4773. [PMID: 5846992]
3.  Skotland, T. and Ljones, T. Direct spectrophotometric detection of ascorbate free radical formed by dopamine β-monooxygenase and by ascorbate oxidase. Biochim. Biophys. Acta 630 (1980) 30–35. [PMID: 7388045]
4.  Evans, J.P., Ahn, K. and Klinman, J.P. Evidence that dioxygen and substrate activation are tightly coupled in dopamine β-monooxygenase. Implications for the reactive oxygen species. J. Biol. Chem. 278 (2003) 49691–49698. [PMID: 12966104]
[EC 1.14.17.1 created 1965 as EC 1.14.2.1, transferred 1972 to EC 1.14.17.1, modified 2020]
 
 
EC 2.8.2.1     
Accepted name: aryl sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + a phenol = adenosine 3′,5′-bisphosphate + an aryl sulfate
Glossary: dopamine.html">dopamine = 4-(2-aminoethyl)benzene-1,2-diol
3′-phosphoadenylyl sulfate = PAPS
Other name(s): phenol sulfotransferase; sulfokinase; 1-naphthol phenol sulfotransferase; 2-naphtholsulfotransferase; 4-nitrocatechol sulfokinase; arylsulfotransferase; dopamine sulfotransferase; p-nitrophenol sulfotransferase; phenol sulfokinase; ritodrine sulfotransferase; PST; 3′-phosphoadenylyl-sulfate:phenol sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:phenol sulfonotransferase
Comments: A number of aromatic compounds can act as acceptors. Organic hydroxylamines are not substrates (cf. EC 2.8.2.9 tyrosine-ester sulfotransferase).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9026-09-9
References:
1.  Romain, Y., Demassieux, S. and Carriere, S. Partial purification and characterization of two isoenzymes involved in the sulfurylation of catecholamines. Biochem. Biophys. Res. Commun. 106 (1982) 999–1005. [DOI] [PMID: 6956338]
2.  Sekura, R. and Jakoby, W.B. Phenol sulfotransferases. J. Biol. Chem. 254 (1979) 5658–5663. [PMID: 447677]
[EC 2.8.2.1 created 1961, modified 1980]
 
 
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]
[EC 3.5.1.76 created 1999]
 
 
EC 3.5.99.12     
Accepted name: salsolinol synthase
Reaction: (R)-salsolinol + H2O = dopamine + acetaldehyde
Glossary: (R)-salsolinol = (+)-salsolinol = (1R)-1,2,3,4-tetrahydro-1-methylisoquinoline-6,7-diol
Other name(s): Sal synthase
Systematic name: (R)-salsolinol dopamine-hydrolase (acetaldehyde-forming)
Comments: The enzyme, present in mammalian brains, forms the catechol isoquinoline (R)-salsolinol. This compound can be metabolized to (R)-N-methylsalsolinol, a 1-methyl-4-phenylpyridinium-like neurotoxin that impairs the function of dopaminergic neurons, causing the clinical symptoms of Parkinson's disease.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Naoi, M., Maruyama, W., Dostert, P., Kohda, K. and Kaiya, T. A novel enzyme enantio-selectively synthesizes (R)-salsolinol, a precursor of a dopaminergic neurotoxin, N-methyl-(R)-salsolinol. Neurosci. Lett. 212 (1996) 183–186. [DOI] [PMID: 8843103]
2.  Naoi, M., Maruyama, W., Takahashi, T., Akao, Y. and Nakagawa, Y. Involvement of endogenous N-methyl-(R)-salsolinol in Parkinson’s disease: induction of apoptosis and protection by (–)deprenyl. J. Neural Transm. Suppl. (2000) 111–121. [DOI] [PMID: 11128601]
3.  Chen, X., Zheng, X., Ali, S., Guo, M., Zhong, R., Chen, Z., Zhang, Y., Qing, H. and Deng, Y. Isolation and sequencing of salsolinol synthase, an enzyme catalyzing salsolinol biosynthesis. ACS Chem Neurosci 9 (2018) 1388–1398. [DOI] [PMID: 29602279]
4.  Xiong, Q., Zheng, X., Wang, J., Chen, Z., Deng, Y., Zhong, R., Wang, J. and Chen, X. Sal synthase induced cytotoxicity of PC12 cells through production of the dopamine metabolites salsolinol and N-methyl-salsolinol. J Integr Neurosci 21:71 (2022). [DOI] [PMID: 35364659]
[EC 3.5.99.12 created 2024]
 
 
EC 3.5.99.14     
Accepted name: (S)-norcoclaurine synthase
Reaction: (S)-norcoclaurine + H2O = dopamine + 4-hydroxyphenylacetaldehyde
For diagram of reaction, click here
Glossary: dopamine.html">dopamine = 4-(2-aminoethyl)benzene-1,2-diol
Other name(s): (S)-norlaudanosoline synthase; 4-hydroxyphenylacetaldehyde hydro-lyase (adding dopamine); 4-hydroxyphenylacetaldehyde hydro-lyase [adding dopamine, (S)-norcoclaurine-forming]
Systematic name: (S)-norcoclaurine dopamine hydrolase (4-hydroxyphenylacetaldehyde-forming)
Comments: The reaction makes a six-membered ring by forming a bond between C-6 of the 3,4-dihydroxyphenyl group of the dopamine and C-1 of the aldehyde in the imine formed between the substrates. The product is the precursor of the benzylisoquinoline alkaloids in plants. The enzyme, formerly known as (S)-norlaudanosoline synthase, will also catalyse the reaction of 4-(2-aminoethyl)benzene-1,2-diol + (3,4-dihydroxyphenyl)acetaldehyde to form (S)-norlaudanosoline, but this alkaloid has not been found to occur in plants.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 79122-01-3
References:
1.  Stadler, R., Zenk, M.H. A revision of the generally accepted pathway for the biosynthesis of the benzyltetrahydroisoquinoline reticuline. Liebigs Ann. Chem. (1990) 555–562. [DOI]
2.  Stadler, R., Kutchan, T.M., Zenk, M.H. (S)-Norcoclaurine is the central intermediate in benzylisoquinoline alkaloid biosynthesis. Phytochemistry 28 (1989) 1083–1086. [DOI]
3.  Samanani, N. and Facchini, P.J. Purification and characterization of norcoclaurine synthase. The first committed enzyme in benzylisoquinoline alkaloid biosynthesis in plants. J. Biol. Chem. 277 (2002) 33878–33883. [DOI] [PMID: 12107162]
[EC 3.5.99.14 created 1984 as EC 4.2.1.78, modified 1999, transferred 2024 to EC 3.5.99.14]
 
 
EC 3.5.99.15     
Accepted name: deacetylisoipecoside synthase
Reaction: deacetylisoipecoside + H2O = dopamine + secologanin
For diagram of indole and ipecac alkaloid biosynthesis, click here
Glossary: dopamine.html">dopamine = 4-(2-aminoethyl)benzene-1,2-diol
Other name(s): deacetylisoipecoside dopamine-lyase; deacetylisoipecoside dopamine-lyase (secologanin-forming)
Systematic name: deacetylisoipecoside dopamine-hydolase (secologanin-forming)
Comments: The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 3.5.99.16, deacetylipecoside synthase. The product is rapidly converted to demethylisoalangiside.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 192827-94-4
References:
1.  DeEknamkul, W., Ounaroon, A., Tanahashi, T., Kutchan, T. and Zenk, M.H. Enzymatic condensation of dopamine and secologanin by cell-free extracts of Alangium lamarckii. Phytochemistry 45 (1997) 477–484. [DOI]
[EC 3.5.99.15 created 2000 as EC 4.3.3.3, transferred 2024 to EC 3.5.99.15]
 
 
EC 3.5.99.16     
Accepted name: deacetylipecoside synthase
Reaction: deacetylipecoside + H2O = dopamine + secologanin
For diagram of indole and ipecac alkaloid biosynthesis, click here
Glossary: dopamine.html">dopamine = 4-(2-aminoethyl)benzene-1,2-diol
Other name(s): deacetylipecoside dopamine-lyase; deacetylipecoside dopamine-lyase (secologanin-forming)
Systematic name: deacetylipecoside dopamine-hydroyase (secologanin-forming)
Comments: The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 3.5.99.15, deacetylisoipecoside synthase. The product is rapidly converted to demethylalangiside.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 192827-93-3
References:
1.  DeEknamkul, W., Ounaroon, A., Tanahashi, T., Kutchan, T. and Zenk, M.H. Enzymatic condensation of dopamine and secologanin by cell-free extracts of Alangium lamarckii. Phytochemistry 45 (1997) 477–484. [DOI]
2.  De-Eknamkul, W., Suttipanta, N. and Kutchan, T.M. Purification and characterization of deacetylipecoside synthase from Alangium lamarckii Thw. Phytochemistry 55 (2000) 177–181. [DOI] [PMID: 11065292]
[EC 3.5.99.16 created 2000 as EC 4.3.3.4, transferred 2024 to EC 3.5.99.16]
 
 
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.html">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 4.1.1.80     
Accepted name: 4-hydroxyphenylpyruvate decarboxylase
Reaction: 4-hydroxyphenylpyruvate = 4-hydroxyphenylacetaldehyde + CO2
For diagram of dopa biosynthesis, click here
Other name(s): 4-hydroxyphenylpyruvate carboxy-lyase
Systematic name: 4-hydroxyphenylpyruvate carboxy-lyase (4-hydroxyphenylacetaldehyde-forming)
Comments: Reacts with dopamine to give the benzylisoquinoline alkaloid skeleton.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 109300-96-1
References:
1.  Rueffer, M. and Zenk, M.H. Distant precursors of benzylisoquinoline alkaloids and their enzymatic formation. Z. Naturforsch. C: Biosci. 42 (1987) 319–332.
[EC 4.1.1.80 created 2002]
 
 
EC 4.1.1.107     
Accepted name: 3,4-dihydroxyphenylacetaldehyde synthase
Reaction: L-dopa + O2 + H2O = 3,4-dihydroxyphenylacetaldehyde + CO2 + NH3 + H2O2
For diagram of phenylacetaldehyde, 4-hydroxyphenylacetaldehyde and 3,4-dihydroxyacetaldehyde biosynthesis, click here
Glossary: L-dopa = 3,4-dihydroxyphenylalanine
Other name(s): DHPAA synthase
Systematic name: L-dopa carboxy-lyase (oxidative-deaminating)
Comments: A pyridoxal 5′-phosphate protein. The enzyme, isolated from the mosquito Aedes aegypti, catalyses the production of 3,4-dihydroxylphenylacetaldehyde directly from L-dopa. Dopamine is not formed as an intermediate (cf. EC 4.1.1.28, aromatic-L-amino-acid decarboxylase). The enzyme is specific for L-dopa and does not react with other aromatic amino acids with the exception of a low activity with α-methyl-L-dopa.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Vavricka, C., Han, Q., Huang, Y., Erickson, S.M., Harich, K., Christensen, B.M. and Li, J. From L-dopa to dihydroxyphenylacetaldehyde: a toxic biochemical pathway plays a vital physiological function in insects. PLoS One 6:e16124 (2011). [DOI] [PMID: 21283636]
[EC 4.1.1.107 created 2017]
 
 
EC 4.2.1.78      
Transferred entry: (S)-norcoclaurine synthase. Now 3.5.99.14, (S)-norcoclaurine synthase
[EC 4.2.1.78 created 1984, modified 1999, deleted 2024]
 
 
EC 4.3.3.3      
Transferred entry: deacetylisoipecoside synthase. Now EC 3.5.99.15, deacetylisoipecoside synthase
[EC 4.3.3.3 created 2000, deleted 2024]
 
 
EC 4.3.3.4      
Transferred entry: deacetylipecoside synthase. Now EC 3.5.99.16, deacetylipecoside synthase
[EC 4.3.3.4 created 2000, deleted 2024]
 
 


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