The Enzyme Database

Your query returned 12 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 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     
Accepted name: (S)-norcoclaurine synthase
Reaction: 4-hydroxyphenylacetaldehyde + dopamine = (S)-norcoclaurine + H2O
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)
Systematic name: 4-hydroxyphenylacetaldehyde hydro-lyase [adding dopamine; (S)-norcoclaurine-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.
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 4.2.1.78 created 1984, modified 1999]
 
 
EC 4.3.3.3     
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
Systematic name: deacetylisoipecoside dopamine-lyase (secologanin-forming)
Comments: The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 4.3.3.4 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.
[EC 4.3.3.3 created 2000]
 
 
EC 4.3.3.4     
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
Systematic name: deacetylipecoside dopamine-lyase (secologanin-forming)
Comments: The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 4.3.3.3 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.
[EC 4.3.3.4 created 2000]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald