EC |
1.11.2.6 |
Accepted name: |
L-tyrosine peroxygenase |
Reaction: |
L-tyrosine + H2O2 = L-dopa + H2O |
Systematic name: |
L-tyrosine:hydrogen-peroxide oxidoreductase (L-dopa-forming) |
Comments: |
The enzyme from the bacterium Streptomyces lincolnensis participates in the biosynthesis of the antibiotic lincomycin A, while that from Streptomyces refuineus is involved in anthramycin biosynthesis. The enzyme, which contains a heme b cofactor, is rapidly inactivated in the presence of hydrogen peroxide, but the presence of L-tyrosine protects it. cf. EC 1.11.2.5, 3-methyl-L-tyrosine peroxygenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Neusser, D., Schmidt, H., Spizek, J., Novotna, J., Peschke, U., Kaschabeck, S., Tichy, P. and Piepersberg, W. The genes lmbB1 and lmbB2 of Streptomyces lincolnensis encode enzymes involved in the conversion of L-tyrosine to propylproline during the biosynthesis of the antibiotic lincomycin A. Arch. Microbiol. 169 (1998) 322–332. [PMID: 9531633] |
2. |
Connor, K.L., Colabroy, K.L. and Gerratana, B. A heme peroxidase with a functional role as an L-tyrosine hydroxylase in the biosynthesis of anthramycin. Biochemistry 50 (2011) 8926–8936. [PMID: 21919439] |
|
[EC 1.11.2.6 created 2020] |
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|
|
|
EC |
1.13.11.29 |
Accepted name: |
stizolobate synthase |
Reaction: |
L-dopa + O2 = 4-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde |
Glossary: |
L-dopa = 3,4-dihydroxy-L-phenylalanine |
Systematic name: |
3,4-dihydroxy-L-phenylalanine:oxygen 4,5-oxidoreductase (recyclizing) |
Comments: |
The intermediate product undergoes ring closure and oxidation, with NAD(P)+ as acceptor, to stizolobic acid. The enzyme requires Zn2+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 65979-39-7 |
References: |
1. |
Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. An enzyme system(s) catalyzing the conversion of dihydroxyphenylalanine into stizolobinic acid and stizolobic acid from etiolated seedlings of Stizolobium hassjoo. Eur. J. Biochem. 68 (1976) 237–243. [DOI] [PMID: 9285] |
2. |
Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. Eur. J. Biochem. 82 (1978) 385–392. [DOI] [PMID: 624278] |
|
[EC 1.13.11.29 created 1978] |
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|
|
|
EC |
1.13.11.30 |
Accepted name: |
stizolobinate synthase |
Reaction: |
L-dopa + O2 = 5-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde |
Glossary: |
L-dopa = 3,4-dihydroxy-L-phenylalanine |
Systematic name: |
3,4-dihydroxy-L-phenylalanine:oxygen 2,3-oxidoreductase (recyclizing) |
Comments: |
The intermediate product undergoes ring closure and oxidation, with NAD(P)+ as acceptor, to stizolobinic acid. The enzyme requires Zn2+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 65979-38-6 |
References: |
1. |
Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. An enzyme system(s) catalyzing the conversion of dihydroxyphenylalanine into stizolobinic acid and stizolobic acid from etiolated seedlings of Stizolobium hassjoo. Eur. J. Biochem. 68 (1976) 237–243. [DOI] [PMID: 9285] |
2. |
Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. Eur. J. Biochem. 82 (1978) 385–392. [DOI] [PMID: 624278] |
|
[EC 1.13.11.30 created 1978] |
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|
|
EC |
1.13.12.15 |
Accepted name: |
3,4-dihydroxyphenylalanine oxidative deaminase |
Reaction: |
2 L-dopa + O2 = 2 3,4-dihydroxyphenylpyruvate + 2 NH3 |
Glossary: |
L-dopa = 3,4-dihydroxy-L-phenylalanine |
Other name(s): |
3,4-dihydroxy-L-phenylalanine: oxidative deaminase; oxidative deaminase; DOPA oxidative deaminase; DOPAODA |
Systematic name: |
3,4-dihydroxy-L-phenylalanine:oxygen oxidoreductase (deaminating) |
Comments: |
This enzyme is one of the three enzymes involved in L-dopa (3,4-dihydroxy-L-phenylalanine) catabolism in the non-oxygenic phototrophic bacterium Rubrivivax benzoatilyticus OU5 (and not Rhodobacter sphaeroides OU5 as had been thought [1]), the other two being EC 4.3.1.22 (dihydroxyphenylalanine reductive deaminase) and EC 2.6.1.49 (3,4-dihydroxyphenylalanine transaminase). In addition to L-dopa, the enzyme can also use L-tyrosine, L-phenylalanine, L-tryptophan and glutamate as substrate, but more slowly. The enzyme is inhibited by NADH and 2-oxoglutarate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Ranjith, N.K., Ramana, Ch.V. and Sasikala, Ch. Purification and characterization of 3,4-dihydroxyphenylalanine oxidative deaminase from Rhodobacter sphaeroides OU5. Can. J. Microbiol. 54 (2008) 829–834. [DOI] [PMID: 18923551] |
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[EC 1.13.12.15 created 2008] |
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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] |
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[EC 1.14.16.2 created 1972, modified 2003, modified 2019] |
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EC |
1.14.18.1 |
Accepted name: |
tyrosinase |
Reaction: |
(1) L-tyrosine + O2 = dopaquinone + H2O (overall reaction) (1a) L-tyrosine + ½ O2 = L-dopa (1b) L-dopa + ½ O2 = dopaquinone + H2O (2) 2 L-dopa + O2 = 2 dopaquinone + 2 H2O |
|
For diagram of melanin biosynthesis, click here |
Other name(s): |
monophenol monooxygenase; phenolase; monophenol oxidase; cresolase; monophenolase; tyrosine-dopa oxidase; monophenol monooxidase; monophenol dihydroxyphenylalanine:oxygen oxidoreductase; N-acetyl-6-hydroxytryptophan oxidase; monophenol, dihydroxy-L-phenylalanine oxygen oxidoreductase; o-diphenol:O2 oxidoreductase; phenol oxidase |
Systematic name: |
L-tyrosine,L-dopa:oxygen oxidoreductase |
Comments: |
A type III copper protein found in a broad variety of bacteria, fungi, plants, insects, crustaceans, and mammals, which is involved in the synthesis of betalains and melanin. The enzyme, which is activated upon binding molecular oxygen, can catalyse both a monophenolase reaction cycle (reaction 1) or a diphenolase reaction cycle (reaction 2). During the monophenolase cycle, one of the bound oxygen atoms is transferred to a monophenol (such as L-tyrosine), generating an o-diphenol intermediate, which is subsequently oxidized to an o-quinone and released, along with a water molecule. The enzyme remains in an inactive deoxy state, and is restored to the active oxy state by the binding of a new oxygen molecule. During the diphenolase cycle the enzyme binds an external diphenol molecule (such as L-dopa) and oxidizes it to an o-quinone that is released along with a water molecule, leaving the enzyme in the intermediate met state. The enzyme then binds a second diphenol molecule and repeats the process, ending in a deoxy state [7]. The second reaction is identical to that catalysed by the related enzyme catechol oxidase (EC 1.10.3.1). However, the latter can not catalyse the hydroxylation or monooxygenation of monophenols. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9002-10-2 |
References: |
1. |
Dawson, C.R. and Tarpley, W.B. The copper oxidases. In: Sumner, J.B. and Myrbäck, K. (Ed.), The Enzymes, 1st edn, vol. 2, Academic Press, New York, 1951, pp. 454–498. |
2. |
Patil, S.S. and Zucker, M. Potato phenolases. Purification and properties. J. Biol. Chem. 240 (1965) 3938–3943. [PMID: 5842066] |
3. |
Pomerantz, S.H. Separation, purification, and properties of two tyrosinases from hamster melanoma. J. Biol. Chem. 238 (1963) 2351–2357. [PMID: 13972077] |
4. |
Robb, D.A. `Tyrosinase. In: Lontie, R. (Ed.), Copper Proteins and Copper Enzymes, vol. 2, CRC Press, Boca Raton, FL, 1984, pp. 207–240. |
5. |
Sanchez-Ferrer, A., Rodriguez-Lopez, J.N., Garcia-Canovas, F. and Garcia-Carmona, F. Tyrosinase: a comprehensive review of its mechanism. Biochim. Biophys. Acta 1247 (1995) 1–11. [DOI] [PMID: 7873577] |
6. |
Steiner, U., Schliemann, W. and Strack, D. Assay for tyrosine hydroxylation activity of tyrosinase from betalain-forming plants and cell cultures. Anal. Biochem. 238 (1996) 72–75. [DOI] [PMID: 8660589] |
7. |
Rolff, M., Schottenheim, J., Decker, H. and Tuczek, F. Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme. Chem Soc Rev 40 (2011) 4077–4098. [DOI] [PMID: 21416076] |
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[EC 1.14.18.1 created 1972, modified 1976, modified 1980 (EC 1.14.17.2 created 1972, incorporated 1984), modified 2012] |
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EC |
2.6.1.49 |
Accepted name: |
dihydroxyphenylalanine transaminase |
Reaction: |
L-dopa + 2-oxoglutarate = 3,4-dihydroxyphenylpyruvate + L-glutamate |
|
For diagram of reaction, click here and for mechanism, click here |
Glossary: |
L-dopa = 3,4-dihydroxy-L-phenylalanine |
Other name(s): |
dopa transaminase; dihydroxyphenylalanine aminotransferase; aspartate-DOPP transaminase (ADT); L-dopa transaminase; dopa aminotransferase; glutamate-DOPP transaminase (GDT); phenylalanine-DOPP transaminase (PDT); DOPA 2-oxoglutarate aminotransferase; DOPAATS |
Systematic name: |
3,4-dihydroxy-L-phenylalanine:2-oxoglutarate aminotransferase |
Comments: |
A pyridoxal-phosphate protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-98-8 |
References: |
1. |
Fonnum, F. and Larsen, K. Purification and properties of dihydroxyphenylalanine transaminase from guinea pig brain. J. Neurochem. 12 (1965) 589–598. [DOI] [PMID: 5829872] |
2. |
Ranjith, N.K., Sasikala, Ch. and Ramana, Ch.V. Catabolism of L-phenylalanine and L-tyrosine by Rhodobacter sphaeroides OU5 occurs through 3,4-dihydroxyphenylalanine. Res. Microbiol. 158 (2007) 506–511. [DOI] [PMID: 17616348] |
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[EC 2.6.1.49 created 1972] |
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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 |
|
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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EC |
4.1.1.84 |
Accepted name: |
D-dopachrome decarboxylase |
Reaction: |
D-dopachrome = 5,6-dihydroxyindole + CO2 |
Glossary: |
D-dopachrome = (2R)-5,6-dioxo-2,3,5,6-tetrahydro-1H-indole-2-carboxylate |
Other name(s): |
phenylpyruvate tautomerase II; D-tautomerase; D-dopachrome tautomerase; D-dopachrome carboxy-lyase |
Systematic name: |
D-dopachrome carboxy-lyase (5,6-dihydroxyindole-forming) |
Comments: |
This enzyme is specific for D-dopachrome as substrate and belongs to the MIF (macrophage migration inhibitory factor) family of proteins. L-Dopachrome, L- or D-α-methyldopachrome and dopaminochrome do not act as substrates (see also EC 5.3.3.12, L-dopachrome isomerase) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 184111-06-6 |
References: |
1. |
Odh, G., Hindemith, A., Rosengren, A.M., Rosengren, E. and Rorsman, H. Isolation of a new tautomerase monitored by the conversion of D-dopachrome to 5,6-dihydroxyindole. Biochem. Biophys. Res. Commun. 197 (1993) 619–624. [DOI] [PMID: 8267597] |
2. |
Yoshida, H., Nishihira, J., Suzuki, M. and Hikichi, K. NMR characterization of physicochemical properties of rat D-dopachrome tautomerase. Biochem. Mol. Biol. Int. 42 (1997) 891–899. [PMID: 9285056] |
3. |
Sugimoto, H., Taniguchi, M., Nakagawa, A., Tanaka, I., Suzuki, M. and Nishihira, J. Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54 Å resolution. Biochemistry 38 (1999) 3268–3279. [DOI] [PMID: 10079069] |
4. |
Nishihira, J., Fujinaga, M., Kuriyama, T., Suzuki, M., Sugimoto, H., Nakagawa, A., Tanaka, I. and Sakai, M. Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal proline is essential for enzyme activation. Biochem. Biophys. Res. Commun. 243 (1998) 538–544. [DOI] [PMID: 9480844] |
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[EC 4.1.1.84 created 2005] |
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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] |
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[EC 4.1.1.107 created 2017] |
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EC |
4.1.1.108 |
Accepted name: |
4-hydroxyphenylacetaldehyde synthase |
Reaction: |
L-tyrosine + O2 + H2O = (4-hydroxyphenyl)acetaldehyde + CO2 + NH3 + H2O2 |
|
For diagram of phenylacetaldehyde, 4-hydroxyphenylacetaldehyde and 3,4-dihydroxyacetaldehyde biosynthesis, click here |
Other name(s): |
TYRDC-2 (gene name) |
Systematic name: |
L-tyrosine carboxy-lyase (oxidative-deaminating) |
Comments: |
A pyridoxal 5′-phosphate protein. The enzyme, isolated from the the plant Petroselinum crispum (parsley), catalyses the production of 4-hydroxyphenylacetaldehyde directly from L-tyrosine. Tyramine is not formed as an intermediate. The enzyme has a low activity with L-dopa (cf. EC 4.1.1.107, 3,4-dihydroxyphenylacetaldehyde synthase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Torrens-Spence, M.P., Gillaspy, G., Zhao, B., Harich, K., White, R.H. and Li, J. Biochemical evaluation of a parsley tyrosine decarboxylase results in a novel 4-hydroxyphenylacetaldehyde synthase enzyme. Biochem. Biophys. Res. Commun. 418 (2012) 211–216. [DOI] [PMID: 22266321] |
2. |
Torrens-Spence, M.P., Liu, P., Ding, H., Harich, K., Gillaspy, G. and Li, J. Biochemical evaluation of the decarboxylation and decarboxylation-deamination activities of plant aromatic amino acid decarboxylases. J. Biol. Chem. 288 (2013) 2376–2387. [DOI] [PMID: 23204519] |
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[EC 4.1.1.108 created 2017] |
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EC
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4.3.1.11
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Deleted entry: | dihydroxyphenylalanine ammonia-lyase. The entry had been drafted on the basis of a single abstract that did not provide experimental evidence of the enzyme-catalysed reaction |
[EC 4.3.1.11 created 1972, deleted 2007] |
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EC |
4.3.1.22 |
Accepted name: |
3,4-dihydroxyphenylalanine reductive deaminase |
Reaction: |
L-dopa + NADH = 3,4-dihydroxyphenylpropanoate + NAD+ + NH3 |
Glossary: |
L-dopa = 3,4-dihydroxy-L-phenylalanine |
Other name(s): |
reductive deaminase; DOPA-reductive deaminase; DOPARDA |
Systematic name: |
3,4-dihydroxy-L-phenylalanine ammonia-lyase (3,4-dihydroxyphenylpropanoate-forming) |
Comments: |
Forms part of the L-phenylalanine-catabolism pathway in the anoxygenic phototrophic bacterium Rhodobacter sphaeroides OU5. NADPH is oxidized more slowly than NADH. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ranjith, N.K., Sasikala, Ch. and Ramana, Ch.V. Catabolism of L-phenylalanine and L-tyrosine by Rhodobacter sphaeroides OU5 occurs through 3,4-dihydroxyphenylalanine. Res. Microbiol. 158 (2007) 506–511. [DOI] [PMID: 17616348] |
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[EC 4.3.1.22 created 2007] |
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EC |
5.3.3.12 |
Accepted name: |
L-dopachrome isomerase |
Reaction: |
L-dopachrome = 5,6-dihydroxyindole-2-carboxylate |
|
For diagram of melanin biosynthesis, click here |
Glossary: |
L-dopachrome = (2S)-5,6-dioxo-2,3,5,6-tetrahydro-1H-indole-2-carboxylate |
Other name(s): |
dopachrome tautomerase; tyrosinase-related protein 2; TRP-1; TRP2; TRP-2; tyrosinase-related protein-2; dopachrome Δ7,Δ2-isomerase; dopachrome Δ-isomerase; dopachrome conversion factor; dopachrome isomerase; dopachrome oxidoreductase; dopachrome-rearranging enzyme; DCF; DCT; dopachrome keto-enol isomerase; L-dopachrome-methyl ester tautomerase |
Systematic name: |
L-dopachrome keto-enol isomerase |
Comments: |
A zinc enzyme. Stereospecific for L-dopachrome. Dopachrome methyl ester is a substrate, but dopaminochrome (2,3-dihydroindole-5,6-quinone) is not (see also EC 4.1.1.84, D-dopachrome decarboxylase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 130122-81-5 |
References: |
1. |
Solano, F., Jiménez-Cervantes, C., Martinez-Liarte, J.H., Garcia-Borrón, J.C. and Lozano, J.A. Molecular mechanism for catalysis by a new zinc enzyme, dopachrome tautomerase. Biochem. J. 313 (1996) 447–453. [PMID: 8573077] |
2. |
Pawelek, J.M. Dopachrome conversion factor functions as an isomerase. Biochem. Biophys. Res. Commun. 166 (1990) 1328–1333. [DOI] [PMID: 2106316] |
3. |
Pennock, J.L., Behnke, J.M., Bickle, Q.D., Devaney, E., Grencis, R.K., Isaac, R.E. , Joshua. G.W., Selkirk. M.E., Zhang. Y. and Meyer, D.J. Rapid purification and characterization of L-dopachrome-methyl ester tautomerase (macrophage-migration-inhibitory factor) from Trichinella spiralis, Trichuris muris and Brugia pahangi. Biochem. J. 335 (1998) 495–498. [PMID: 9794786] |
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[EC 5.3.3.12 created 1992, modified 1999, modified 2005] |
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