EC |
1.2.1.67 |
Accepted name: |
vanillin dehydrogenase |
Reaction: |
vanillin + NAD+ + H2O = vanillate + NADH + 2 H+ |
Glossary: |
vanillate = 4-hydroxy-3-methoxybenzoate
vanillin = 4-hydroxy-3-methoxybenzaldehyde |
Systematic name: |
vanillin:NAD+ oxidoreductase |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 189767-93-9 |
References: |
1. |
Pometto, A.L. and Crawford, D.L. Whole-cell bioconversion of vanillin to vanillic acid by Streptomyces viridosporus. Appl. Environ. Microbiol. 45 (1983) 1582–1585. [PMID: 6870241] |
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[EC 1.2.1.67 created 2000] |
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EC |
1.11.1.16 |
Accepted name: |
versatile peroxidase |
Reaction: |
(1) 1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O (2) 2 manganese(II) + 2 H+ + H2O2 = 2 manganese(III) + 2 H2O |
Glossary: |
4-hydroxy-3-methoxybenzaldehyde = vanillin
2-methoxyphenol = guaiacol |
Other name(s): |
VP; hybrid peroxidase; polyvalent peroxidase; reactive-black-5:hydrogen-peroxide oxidoreductase |
Systematic name: |
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol:hydrogen-peroxide oxidoreductase |
Comments: |
A hemoprotein. This ligninolytic peroxidase combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, EC 1.11.1.13, manganese peroxidase and EC 1.11.1.14, lignin peroxidase. Unlike these two enzymes, it is also able to oxidize phenols, hydroquinones and both low- and high-redox-potential dyes, due to a hybrid molecular architecture that involves multiple binding sites for substrates [2,4]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 42613-30-9, 114995-15-2 |
References: |
1. |
Martínez, M.J., Ruiz-Dueñas, F.J., Guillén, F. and Martínez, A.T. Purification and catalytic properties of two manganese peroxidase
isoenzymes from Pleurotus eryngii. Eur. J. Biochem. 237 (1996) 424–432. [DOI] [PMID: 8647081] |
2. |
Heinfling, A., Ruiz-Dueñas, F.J., Martínez, M.J., Bergbauer, M., Szewzyk, U. and Martínez, A.T. A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta. FEBS Lett. 428 (1998) 141–146. [DOI] [PMID: 9654123] |
3. |
Ruiz-Dueñas, F.J., Martínez, M.J. and Martínez, A.T. Molecular characterization of a novel peroxidase isolated from the
ligninolytic fungus Pleurotus eryngii. Mol. Microbiol. 31 (1999) 223–235. [DOI] [PMID: 9987124] |
4. |
Camarero, S., Sarkar, S., Ruiz-Dueñas, F.J., Martínez, M.J. and Martínez, A.T. Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites. J. Biol. Chem. 274 (1999) 10324–10330. [DOI] [PMID: 10187820] |
5. |
Ruiz-Dueñas, F.J., Martínez, M.J. and Martínez, A.T. Heterologous expression of Pleurotus eryngii peroxidase confirms its
ability to oxidize Mn2+ and different aromatic substrates. Appl. Environ. Microbiol. 65 (1999) 4705–4707. [PMID: 10508113] |
6. |
Camarero, S., Ruiz-Dueñas, F.J., Sarkar, S., Martínez, M.J. and Martínez, A.T. The cloning of a new peroxidase found in lignocellulose cultures of
Pleurotus eryngii and sequence comparison with other fungal peroxidases. FEMS Microbiol. Lett. 191 (2000) 37–43. [DOI] [PMID: 11004397] |
7. |
Ruiz-Dueñas, F.J., Camarero, S., Pérez-Boada, M., Martínez, M.J. and Martínez, A.T. A new versatile peroxidase from Pleurotus. Biochem. Soc. Trans. 29 (2001) 116–122. [PMID: 11356138] |
8. |
Banci, L., Camarero, S., Martínez, A.T., Martínez, M.J., Pérez-Boada, M., Pierattelli, R. and Ruiz-Dueñas, F.J. NMR study of manganese(II) binding by a new versatile peroxidase from the
white-rot fungus Pleurotus eryngii. J. Biol. Inorg. Chem. 8 (2003) 751–760. [DOI] [PMID: 12884090] |
9. |
Pérez-Boada, M., Ruiz-Dueñas, F.J., Pogni, R., Basosi, R., Choinowski, T., Martínez, M.J., Piontek, K. and Martínez, A.T. Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways. J. Mol. Biol. 354 (2005) 385–402. [DOI] [PMID: 16246366] |
10. |
Caramelo, L., Martínez, M.J. and Martínez, A.T. A search for ligninolytic peroxidases in the fungus Pleurotus eryngii involving α-keto-γ-thiomethylbutyric acid and lignin model dimer. Appl. Environ. Microbiol. 65 (1999) 916–922. [PMID: 10049842] |
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[EC 1.11.1.16 created 2006, modified 2016] |
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EC
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4.1.2.41
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Transferred entry: | vanillin synthase. Now included with EC 4.1.2.61, feruloyl-CoA hydratase/lyase
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[EC 4.1.2.41 created 2000, deleted 2019] |
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EC |
4.1.2.65 |
Accepted name: |
ferulate hydratase/lyase |
Reaction: |
ferulate + H2O = vanillin + acetate (overall reaction) (1a) ferulate + H2O = 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoate (1b) 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoate = vanillin + acetate |
Glossary: |
ferulate = 4-hydroxy-3-methoxycinnamate
vanillin = 4-hydroxy-3-methoxybenzaldehyde
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Other name(s): |
vanillin synthase; VpVan; VAN; ferulate aldolase |
Systematic name: |
ferulate acetate-lyase (vanillin-forming) |
Comments: |
The enzyme is located in the chloroplasts of vanilla pods of the orchid Vanilla planifolia. It also converts ferulic acid 4-O-β-D-glucopyranoside to vanillin 4-O-β-D-glucopyranoside. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Gallage, N.J., Hansen, E.H., Kannangara, R., Olsen, C.E., Motawia, M.S., Jørgensen, K., Holme, I., Hebelstrup, K., Grisoni, M. and Møller, B.L. Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme. Nat. Commun. 5:4037 (2014). [DOI] [PMID: 24941968] |
2. |
Kundu, A. Vanillin biosynthetic pathways in plants. Planta 245 (2017) 1069–1078. [DOI] [PMID: 28357540] |
3. |
Gallage, N.J., Jørgensen, K., Janfelt, C., Nielsen, A.JZ., Naake, T., Dunski, E., Dalsten, L., Grisoni, M. and Møller, B.L. The intracellular localization of the vanillin biosynthetic machinery in pods of Vanilla planifolia. Plant Cell Physiol. 59 (2018) 304–318. [DOI] [PMID: 29186560] |
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[EC 4.1.2.65 created 2024] |
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