The Enzyme Database

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EC 1.11.1.7     
Accepted name: peroxidase
Reaction: 2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O
Other name(s): lactoperoxidase; guaiacol peroxidase; plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxidase; heme peroxidase; oxyperoxidase; protoheme peroxidase; pyrocatechol peroxidase; scopoletin peroxidase; Coprinus cinereus peroxidase; Arthromyces ramosus peroxidase
Systematic name: phenolic donor:hydrogen-peroxide oxidoreductase
Comments: Heme proteins with histidine as proximal ligand. The iron in the resting enzyme is Fe(III). They also peroxidize non-phenolic substrates such as 3,3′,5,5′-tetramethylbenzidine (TMB) and 2,2′-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS). Certain peroxidases (e.g. lactoperoxidase, SBP) oxidize bromide, iodide and thiocyanate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9003-99-0
References:
1.  Kenten, R.H. and Mann, P.J.G. Simple method for the preparation of horseradish peroxidase. Biochem. J. 57 (1954) 347–348. [PMID: 13172193]
2.  Morrison, M., Hamilton, H.B. and Stotz, E. The isolation and purification of lactoperoxidase by ion exchange chromatography. J. Biol. Chem. 228 (1957) 767–776. [PMID: 13475358]
3.  Paul, K.G. Peroxidases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 227–274.
4.  Tagawa, K., Shin, M. and Okunuki, K. Peroxidases from wheat germ. Nature (Lond.) 183 (1959) 111. [PMID: 13622706]
5.  Theorell, H. The preparation and some properties of crystalline horse-radish peroxidase. Ark. Kemi Mineral. Geol. 16A No. 2 (1943) 1–11.
6.  Farhangrazi, Z.S., Copeland, B.R., Nakayama, T., Amachi, T., Yamazaki, I. and Powers, L.S. Oxidation-reduction properties of compounds I and II of Arthromyces ramosus peroxidase. Biochemistry 33 (1994) 5647–5652. [PMID: 8180190]
7.  Aitken, M.D. and Heck, P.E. Turnover capacity of coprinus cinereus peroxidase for phenol and monosubstituted phenol. Biotechnol. Prog. 14 (1998) 487–492. [DOI] [PMID: 9622531]
8.  Dunford, H.B. Heme peroxidases, Wiley-VCH, New York, 1999, pp. 33–218.
9.  Torres, E and Ayala, M. Biocatalysis based on heme peroxidases, Springer, Berlin, 2010, pp. 7–110.
[EC 1.11.1.7 created 1961, modified 2011]
 
 
EC 1.14.11.60     
Accepted name: scopoletin 8-hydroxylase
Reaction: scopoletin + 2-oxoglutarate + O2 = fraxetin + succinate + CO2
Glossary: fraxetin = 7,8-dihydroxy-6-methoxy-2H-chromen-2-one
scopoletin = 7-hydroxy-6-methoxy-2H-chromen-2-one
Other name(s): S8H (gene name)
Systematic name: scopoletin,2-oxoglutarate:oxygen oxidoreductase (8-hydroxylating)
Comments: Requires iron(II) and ascorbate. A protein involved in biosynthesis of iron(III)-chelating coumarins in higher plants.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Siwinska, J., Siatkowska, K., Olry, A., Grosjean, J., Hehn, A., Bourgaud, F., Meharg, A.A., Carey, M., Lojkowska, E. and Ihnatowicz, A. Scopoletin 8-hydroxylase: a novel enzyme involved in coumarin biosynthesis and iron-deficiency responses in Arabidopsis. J. Exp. Bot. 69 (2018) 1735–1748. [PMID: 29361149]
2.  Rajniak, J., Giehl, R.FH., Chang, E., Murgia, I., von Wiren, N. and Sattely, E.S. Biosynthesis of redox-active metabolites in response to iron deficiency in plants. Nat. Chem. Biol. 14 (2018) 442–450. [PMID: 29581584]
[EC 1.14.11.60 created 2018]
 
 
EC 1.14.11.61     
Accepted name: feruloyl-CoA 6-hydroxylase
Reaction: trans-feruloyl-CoA + 2-oxoglutarate + O2 = trans-6-hydroxyferuloyl-CoA + succinate + CO2
Glossary: trans-feruloyl-CoA = 4-hydroxy-3-methoxycinnamoyl-CoA = (E)-3-(4-hydroxy-3-methoxyphenyl)propenoyl-CoA
Systematic name: feruloyl-CoA,2-oxoglutarate:oxygen oxidoreductase (6-hydroxylating)
Comments: Requires iron(II) and ascorbate. The product spontaneously undergoes trans-cis isomerization and lactonization to form scopoletin, liberating CoA in the process. The enzymes from the plants Ruta graveolens and Ipomoea batatas also act on trans-4-coumaroyl-CoA. cf. EC 1.14.11.62, trans-4-coumaroyl-CoA 2-hydroxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kai, K., Mizutani, M., Kawamura, N., Yamamoto, R., Tamai, M., Yamaguchi, H., Sakata, K. and Shimizu, B. Scopoletin is biosynthesized via ortho-hydroxylation of feruloyl CoA by a 2-oxoglutarate-dependent dioxygenase in Arabidopsis thaliana. Plant J. 55 (2008) 989–999. [PMID: 18547395]
2.  Bayoumi, S.A., Rowan, M.G., Blagbrough, I.S. and Beeching, J.R. Biosynthesis of scopoletin and scopolin in cassava roots during post-harvest physiological deterioration: the E-Z-isomerisation stage. Phytochemistry 69 (2008) 2928–2936. [PMID: 19004461]
3.  Vialart, G., Hehn, A., Olry, A., Ito, K., Krieger, C., Larbat, R., Paris, C., Shimizu, B., Sugimoto, Y., Mizutani, M. and Bourgaud, F. A 2-oxoglutarate-dependent dioxygenase from Ruta graveolens L. exhibits p-coumaroyl CoA 2′-hydroxylase activity (C2′H): a missing step in the synthesis of umbelliferone in plants. Plant J. 70 (2012) 460–470. [DOI] [PMID: 22168819]
4.  Matsumoto, S., Mizutani, M., Sakata, K. and Shimizu, B. Molecular cloning and functional analysis of the ortho-hydroxylases of p-coumaroyl coenzyme A/feruloyl coenzyme A involved in formation of umbelliferone and scopoletin in sweet potato, Ipomoea batatas (L.) Lam. Phytochemistry 74 (2012) 49–57. [PMID: 22169019]
[EC 1.14.11.61 created 2019]
 
 
EC 1.14.11.62     
Accepted name: trans-4-coumaroyl-CoA 2-hydroxylase
Reaction: trans-4-coumaroyl-CoA + 2-oxoglutarate + O2 = 2,4-dihydroxycinnamoyl-CoA + succinate + CO2
Glossary: trans-4-coumaroyl-CoA = (2E)-3-(4-hydroxyphenyl)prop-2-enoyl-CoA
2,4-dihydroxycinnamoyl-CoA = (2E)-3-(2,4-dihydroxyphenyl)prop-2-enoyl-CoA
umbelliferone = 7-hydroxycoumarin
Other name(s): Diox4 (gene name); C2′H (gene name)
Systematic name: (2E)-3-(4-hydroxyphenyl)prop-2-enoyl-CoA,2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating)
Comments: Requires iron(II) and ascorbate. The product spontaneously undergoes trans-cis isomerization followed by lactonization and cyclization, liberating CoA and forming umbelliferone. The enzymes from the plants Ruta graveolens and Ipomoea batatas also act on trans-feruloyl-CoA (cf. EC 1.14.11.61, feruloyl-CoA 6-hydroxylase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Vialart, G., Hehn, A., Olry, A., Ito, K., Krieger, C., Larbat, R., Paris, C., Shimizu, B., Sugimoto, Y., Mizutani, M. and Bourgaud, F. A 2-oxoglutarate-dependent dioxygenase from Ruta graveolens L. exhibits p-coumaroyl CoA 2′-hydroxylase activity (C2′H): a missing step in the synthesis of umbelliferone in plants. Plant J. 70 (2012) 460–470. [DOI] [PMID: 22168819]
2.  Matsumoto, S., Mizutani, M., Sakata, K. and Shimizu, B. Molecular cloning and functional analysis of the ortho-hydroxylases of p-coumaroyl coenzyme A/feruloyl coenzyme A involved in formation of umbelliferone and scopoletin in sweet potato, Ipomoea batatas (L.) Lam. Phytochemistry 74 (2012) 49–57. [PMID: 22169019]
[EC 1.14.11.62 created 2019]
 
 
EC 2.4.1.104     
Accepted name: o-dihydroxycoumarin 7-O-glucosyltransferase
Reaction: UDP-glucose + 7,8-dihydroxycoumarin = UDP + daphnin
Other name(s): uridine diphosphoglucose-o-dihydroxycoumarin 7-O-glucosyltransferase; UDP-glucose:o-dihydroxycoumarin glucosyltransferase
Systematic name: UDP-glucose:7,8-dihydroxycoumarin 7-O-β-D-glucosyltransferase
Comments: Converts the aglycone daphetin into daphnin and, more slowly, esculetin into cichoriin, umbelliferone into skimmin, hydrangetin into hydrangin and scopoletin into scopolin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74114-37-7
References:
1.  Ibrahim, R.K. and Boulay, B. Purification and some properties of UDP-glucose:o-hydroxycoumarin 7-O-glucosyltransferase from tobacco cell cultures. Plant Sci. Lett. 18 (1980) 177–184.
[EC 2.4.1.104 created 1983]
 
 
EC 2.4.1.128     
Accepted name: scopoletin glucosyltransferase
Reaction: UDP-glucose + scopoletin = UDP + scopolin
Other name(s): uridine diphosphoglucose-scopoletin glucosyltransferase; UDP-glucose:scopoletin glucosyltransferase; SGTase
Systematic name: UDP-glucose:scopoletin O-β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81210-69-7
References:
1.  Hino, F., Okazaki, M. and Miura, Y. Effect of 2,4-dichlorophenoxyacetic acid on glucosylation of scopoletin to scopolin in tobacco tissue-culture. Plant Physiol. 69 (1982) 810–813. [PMID: 16662301]
[EC 2.4.1.128 created 1984]
 
 


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