The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version



EC 1.13.11.1     
Accepted name: catechol 1,2-dioxygenase
Reaction: catechol + O2 = cis,cis-muconate
For diagram of benzoate metabolism, click here
Other name(s): catechol-oxygen 1,2-oxidoreductase; 1,2-pyrocatechase; catechase; catechol 1,2-oxygenase; catechol dioxygenase; pyrocatechase; pyrocatechol 1,2-dioxygenase; CD I; CD II
Systematic name: catechol:oxygen 1,2-oxidoreductase
Comments: Requires Fe3+. Involved in the metabolism of nitro-aromatic compounds by a strain of Pseudomonas putida.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9027-16-1
References:
1.  Hayaishi, O. Direct oxygenation by O2, oxygenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 353–371.
2.  Hayaishi, O., Katagiri, M. and Rothberg, S. Studies on oxygenases: pyrocatechase. J. Biol. Chem. 229 (1957) 905–920. [PMID: 13502352]
3.  Sistrom, W.R. and Stanier, R.Y. The mechanism of formation of β-ketoadipic acid by bacteria. J. Biol. Chem. 210 (1954) 821–836. [PMID: 13211620]
4.  Zeyer, J., Kocher, H.P. and Timmis, N. Influence of para-substituents on the oxidative metabolism of o-nitrophenols by Pseudomonas putida B2. Appl. Environ. Microbiol. 52 (1986) 334–339. [PMID: 3752997]
[EC 1.13.11.1 created 1961 as EC 1.99.2.2, transferred 1965 to EC 1.13.1.1, transferred 1972 to EC 1.13.11.1]
 
 
EC 1.13.11.10     
Accepted name: 7,8-dihydroxykynurenate 8,8a-dioxygenase
Reaction: 7,8-dihydroxykynurenate + O2 = 5-(3-carboxy-3-oxopropenyl)-4,6-dihydroxypyridine-2-carboxylate
Other name(s): 7,8-dihydroxykynurenate oxygenase; 7,8-dihydroxykynurenate 8,8α-dioxygenase; 7,8-dihydroxykynurenate:oxygen 8,8a-oxidoreductase (decyclizing)
Systematic name: 7,8-dihydroxykynurenate:oxygen 8,8a-oxidoreductase (ring-opening)
Comments: Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9029-58-7
References:
1.  Kuno, S., Tashiro, M., Taniuchi, H., Horibata, K., Hayaishi, O., Seno, S., Tokuyama, T. and Sakan, T. Enzymatic degradation of kynurenic acid. Fed. Proc. 20 (1961) 3.
[EC 1.13.11.10 created 1965 as EC 1.13.1.10, transferred 1972 to EC 1.13.11.10]
 
 
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 1.13.11.12     
Accepted name: linoleate 13S-lipoxygenase
Reaction: (1) linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
(2) α-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
Glossary: linoleate = (9Z,12Z)-octadeca-9,12-dienoate
α-linolenate = (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
Other name(s): 13-lipoxidase; carotene oxidase; 13-lipoperoxidase; fat oxidase; 13-lipoxydase; lionoleate:O2 13-oxidoreductase
Systematic name: linoleate:oxygen 13-oxidoreductase
Comments: Contains nonheme iron. A common plant lipoxygenase that oxidizes linoleate and α-linolenate, the two most common polyunsaturated fatty acids in plants, by inserting molecular oxygen at the C-13 position with (S)-configuration. This enzyme produces precursors for several important compounds, including the plant hormone jasmonic acid. EC 1.13.11.58, linoleate 9S-lipoxygenase, catalyses a similar reaction at the second available position of these fatty acids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-60-1
References:
1.  Christopher, J., Pistorius, E. and Axelrod, B. Isolation of an enzyme of soybean lipoxidase. Biochim. Biophys. Acta 198 (1970) 12–19. [DOI] [PMID: 5461103]
2.  Theorell, H., Holman, R.T. and Åkesson, Å. Crystalline lipoxidase. Acta Chem. Scand. 1 (1947) 571–576. [PMID: 18907700]
3.  Zimmerman, D.C. Specificity of flaxseed lipoxidase. Lipids 5 (1970) 392–397. [DOI] [PMID: 5447012]
4.  Royo, J., Vancanneyt, G., Perez, A.G., Sanz, C., Stormann, K., Rosahl, S. and Sanchez-Serrano, J.J. Characterization of three potato lipoxygenases with distinct enzymatic activities and different organ-specific and wound-regulated expression patterns. J. Biol. Chem. 271 (1996) 21012–21019. [DOI] [PMID: 8702864]
5.  Bachmann, A., Hause, B., Maucher, H., Garbe, E., Voros, K., Weichert, H., Wasternack, C. and Feussner, I. Jasmonate-induced lipid peroxidation in barley leaves initiated by distinct 13-LOX forms of chloroplasts. Biol. Chem. 383 (2002) 1645–1657. [DOI] [PMID: 12452441]
[EC 1.13.11.12 created 1961 as EC 1.99.2.1, transferred 1965 to EC 1.13.1.13, transferred 1972 to EC 1.13.11.12, modified 2011, modified 2012]
 
 
EC 1.13.11.13      
Deleted entry: ascorbate 2,3-dioxygenase. The activity is the sum of several enzymatic and spontaneous reactions
[EC 1.13.11.13 created 1972, deleted 2012]
 
 
EC 1.13.11.14     
Accepted name: 2,3-dihydroxybenzoate 3,4-dioxygenase
Reaction: 2,3-dihydroxybenzoate + O2 = 3-carboxy-2-hydroxymuconate semialdehyde
Other name(s): o-pyrocatechuate oxygenase; 2,3-dihydroxybenzoate 1,2-dioxygenase; 2,3-dihydroxybenzoic oxygenase; 2,3-dihydroxybenzoate oxygenase; 2,3-dihydroxybenzoate:oxygen 3,4-oxidoreductase (decyclizing)
Systematic name: 2,3-dihydroxybenzoate:oxygen 3,4-oxidoreductase (ring-opening)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9032-31-9
References:
1.  Ribbons, D.W. Bacterial oxidation of 2,3-dihydroxybenzoic acid - a new oxygenase. Biochem. J. 99 (1966) 30.
[EC 1.13.11.14 created 1972, modified 1976]
 
 
EC 1.13.11.15     
Accepted name: 3,4-dihydroxyphenylacetate 2,3-dioxygenase
Reaction: 3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde
Other name(s): 3,4-dihydroxyphenylacetic acid 2,3-dioxygenase; HPC dioxygenase; homoprotocatechuate 2,3-dioxygenase; 3,4-dihydroxyphenylacetate:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: 3,4-dihydroxyphenylacetate:oxygen 2,3-oxidoreductase (ring-opening)
Comments: An iron protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 37256-56-7
References:
1.  Adachi, K., Takeda, Y., Senoh, S. and Kita, H. Metabolism of p-hydroxyphenylacetic acid in Pseudomonas ovalis. Biochim. Biophys. Acta 93 (1964) 483–493. [DOI] [PMID: 14263147]
2.  Barbour, M.G. and Bayly, R.C. Control of meta-cleavage degradation of 4-hydroxyphenylacetate in Pseudomonas putida. J. Bacteriol. 147 (1981) 844–850. [PMID: 6895079]
3.  Krishnan Kutty, R., Devi, N.A., Veeraswamy, M., Ramesh, S. and Subba Rao, P.V. Degradation of (±)-synephrine by Arthrobacter synephrinum. Oxidation of 3,4-dihydroxyphenylacetate to 2-hydroxy-5-carboxymethyl-muconate semialdehyde. Biochem. J. 167 (1977) 163–170. [PMID: 588248]
[EC 1.13.11.15 created 1972]
 
 
EC 1.13.11.16     
Accepted name: 3-carboxyethylcatechol 2,3-dioxygenase
Reaction: (1) 3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
(2) (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate
For diagram of 3-phenylpropanoate catabolism, click here and for diagram of cinnamate catabolism, click here
Glossary: (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate = trans-2,3-dihydroxycinnamate
Other name(s): 2,3-dihydroxy-β-phenylpropionic dioxygenase; 2,3-dihydroxy-β-phenylpropionate oxygenase; 3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase; 3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase (decyclizing)
Systematic name: 3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase (ring-opening)
Comments: An iron protein. This enzyme catalyses a step in the pathway of phenylpropanoid compounds degradation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 105503-63-7
References:
1.  Dagley, S., Chapman, P.J. and Gibson, D.T. The metabolism of β-phenylpropionic acid by an Achromobacter. Biochem. J. 97 (1965) 643–650. [PMID: 5881653]
2.  Lam, W. W. Y and Bugg, T. D. H. Chemistry of extradiol aromatic ring cleavage: isolation of a stable dienol ring fission intermediate and stereochemistry of its enzymatic hydrolytic clevage. J. Chem. Soc., Chem. Commun. 10 (1994) 1163–1164.
3.  Díaz, E., Ferrández, A. and García, J.L. Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12. J. Bacteriol. 180 (1998) 2915–2923. [PMID: 9603882]
[EC 1.13.11.16 created 1972, modified 2011, modified 2012]
 
 
EC 1.13.11.17     
Accepted name: indole 2,3-dioxygenase
Reaction: indole + O2 = 2-formylaminobenzaldehyde
Other name(s): indole oxidase; indoleamine 2,3-dioxygenase (ambiguous); indole:O2 oxidoreductase; indole-oxygen 2,3-oxidoreductase (decyclizing); IDO (ambiguous); indole:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: indole:oxygen 2,3-oxidoreductase (ring-opening)
Comments: Enzymes from the plants Tecoma stans, Jasminum grandiflorum and Zea mays are flavoproteins containing copper. They are part of enzyme systems that form either anthranil (2,1-benzoisoxazole) (Tecoma stans), anthranilate (Jasminum grandiflorum) or both (Zea mays) as the final product. A second enzyme from Tecoma stans is not a flavoprotein, does not require copper, and is part of a system that forms anthranilate as the final product.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-57-8
References:
1.  Nair, P.M. and Vaidyanathan, C.S. An indole oxidase isolated from the leaves of Tecoma stans. Biochim. Biophys. Acta 81 (1964) 496–506. [PMID: 14170321]
2.  Chauhan, Y.S., Rathore, V.S., Garg, G.K. and Bhargava, A. Detection of an indole oxidizing system in maize leaves. Biochem. Biophys. Res. Commun. 83 (1978) 1237–1245. [DOI] [PMID: 697856]
3.  Divakar, N.G., Subramanian, V., Sugumaran, M. and Vaidyanathan, C.S. Indole oxygenase from the leaves of Jasminum grandiflorum. Plant Sci. Lett. 15 (1979) 177–181.
4.  Kunapuli, S.P. and Vaidyanathan, C.S. Purification and characterization of a new indole oxygenase from the leaves of Tecoma stans L. Plant Physiol. 71 (1983) 19–23. [PMID: 16662784]
[EC 1.13.11.17 created 1972, modified 1986]
 
 
EC 1.13.11.18     
Accepted name: persulfide dioxygenase
Reaction: S-sulfanylglutathione + O2 + H2O = glutathione + sulfite + 2 H+ (overall reaction)
(1a) S-sulfanylglutathione + O2 = S-sulfinatoglutathione + H+
(1b) S-sulfinatoglutathione + H2O = glutathione + sulfite + H+ (spontaneous)
Other name(s): sulfur oxygenase (incorrect); sulfur:oxygen oxidoreductase (incorrect); sulfur dioxygenase (incorrect)
Systematic name: S-sulfanylglutathione:oxygen oxidoreductase
Comments: An iron protein. Perthiols, formed spontaneously by interactions between thiols and elemental sulfur or sulfide, are the only acceptable substrate to the enzyme. The sulfite that is formed by the enzyme can be further converted into sulfate, thiosulfate or S-sulfoglutathione (GSSO3-) non-enzymically [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-58-9
References:
1.  Suzuki, I. and Silver, M. The initial product and properties of the sulfur-oxidizing enzyme of thiobacilli. Biochim. Biophys. Acta 122 (1966) 22–33. [PMID: 5968172]
2.  Rohwerder, T. and Sand, W. The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp. Microbiology 149 (2003) 1699–1710. [DOI] [PMID: 12855721]
3.  Liu, H., Xin, Y. and Xun, L. Distribution, diversity, and activities of sulfur dioxygenases in heterotrophic bacteria. Appl. Environ. Microbiol. 80 (2014) 1799–1806. [DOI] [PMID: 24389926]
4.  Holdorf, M.M., Owen, H.A., Lieber, S.R., Yuan, L., Adams, N., Dabney-Smith, C. and Makaroff, C.A. Arabidopsis ETHE1 encodes a sulfur dioxygenase that is essential for embryo and endosperm development. Plant Physiol. 160 (2012) 226–236. [DOI] [PMID: 22786886]
5.  Pettinati, I., Brem, J., McDonough, M.A. and Schofield, C.J. Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy. Hum. Mol. Genet. 24 (2015) 2458–2469. [DOI] [PMID: 25596185]
[EC 1.13.11.18 created 1972, modified 2015]
 
 
EC 1.13.11.19     
Accepted name: cysteamine dioxygenase
Reaction: 2-aminoethanethiol + O2 = hypotaurine
For diagram of taurine biosynthesis, click here
Other name(s): persulfurase; cysteamine oxygenase; cysteamine:oxygen oxidoreductase
Systematic name: 2-aminoethanethiol:oxygen oxidoreductase
Comments: A non-heme iron protein that is involved in the biosynthesis of taurine. Requires catalytic amounts of a cofactor-like compound, such as sulfur, sufide, selenium or methylene blue for maximal activity. 3-Aminopropanethiol (homocysteamine) and 2-mercaptoethanol can also act as substrates, but glutathione, cysteine, and cysteine ethyl- and methyl esters are not good substrates [1,3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-41-4
References:
1.  Cavallini, D., de Marco, C., Scandurra, R., Duprè, S. and Graziani, M.T. The enzymatic oxidation of cysteamine to hypotaurine. Purification and properties of the enzyme. J. Biol. Chem. 241 (1966) 3189–3196. [PMID: 5912113]
2.  Wood, J.L. and Cavallini, D. Enzymic oxidation of cysteamine to hypotaurine in the absence of a cofactor. Arch. Biochem. Biophys. 119 (1967) 368–372. [DOI] [PMID: 6052430]
3.  Cavallini, D., Federici, G., Ricci, G., Duprè, S. and Antonucci, A. The specificity of cysteamine oxygenase. FEBS Lett. 56 (1975) 348–351. [DOI] [PMID: 1157952]
4.  Richerson, R.B. and Ziegler, D.M. Cysteamine dioxygenase. Methods Enzymol. 143 (1987) 410–415. [DOI] [PMID: 3657558]
[EC 1.13.11.19 created 1972, modified 2006]
 
 


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