The Enzyme Database

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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]
[EC 1.2.1.67 created 2000]
 
 
EC 1.2.3.12      
Transferred entry: vanillate demethylase. Now EC 1.14.13.82, vanillate monooxygenase
[EC 1.2.3.12 created 2000, deleted 2003]
 
 
EC 1.14.13.82     
Accepted name: vanillate monooxygenase
Reaction: vanillate + O2 + NADH + H+ = 3,4-dihydroxybenzoate + NAD+ + H2O + formaldehyde
Glossary: vanillate = 4-hydroxy-3-methoxybenzoate
Other name(s): 4-hydroxy-3-methoxybenzoate demethylase; vanillate demethylase
Systematic name: vanillate:oxygen oxidoreductase (demethylating)
Comments: Forms part of the vanillin degradation pathway in Arthrobacter sp.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 39307-11-4
References:
1.  Brunel, F. and Davison, J. Cloning and sequencing of Pseudomonas genes encoding vanillate demethylase. J. Bacteriol. 170 (1988) 4924–4930. [DOI] [PMID: 3170489]
2.  Priefert, H., Rabenhorst, J. and Steinbuchel, A. Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate. J. Bacteriol. 179 (1997) 2595–2607. [DOI] [PMID: 9098058]
[EC 1.14.13.82 created 2000 as EC 1.2.3.12, transferred 2003 to EC 1.14.13.82]
 
 
EC 2.1.1.341     
Accepted name: vanillate/3-O-methylgallate O-demethylase
Reaction: (1) vanillate + tetrahydrofolate = protocatechuate + 5-methyltetrahydrofolate
(2) 3-O-methylgallate + tetrahydrofolate = gallate + 5-methyltetrahydrofolate
Glossary: protocatechuate = 3,4-dihydroxybenzoate
vanillate = 4-hydroxy-3-methoxybenzoate
gallate = 3,4,5-trihydroxybenzoate
Other name(s): ligM (gene name)
Systematic name: vanillate:tetrahydrofolate O-methyltransferase
Comments: The enzyme, characterized from the bacterium Sphingomonas sp. SYK6, is involved in the degradation of lignin. The enzyme has similar activities with vanillate and 3-O-methylgallate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Nishikawa, S., Sonoki, T., Kasahara, T., Obi, T., Kubota, S., Kawai, S., Morohoshi, N. and Katayama, Y. Cloning and sequencing of the Sphingomonas (Pseudomonas) paucimobilis gene essential for the O demethylation of vanillate and syringate. Appl. Environ. Microbiol. 64 (1998) 836–842. [PMID: 9501423]
2.  Masai, E., Sasaki, M., Minakawa, Y., Abe, T., Sonoki, T., Miyauchi, K., Katayama, Y. and Fukuda, M. A novel tetrahydrofolate-dependent O-demethylase gene is essential for growth of Sphingomonas paucimobilis SYK-6 with syringate. J. Bacteriol. 186 (2004) 2757–2765. [DOI] [PMID: 15090517]
3.  Abe, T., Masai, E., Miyauchi, K., Katayama, Y. and Fukuda, M. A tetrahydrofolate-dependent O-demethylase, LigM, is crucial for catabolism of vanillate and syringate in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 187 (2005) 2030–2037. [DOI] [PMID: 15743951]
[EC 2.1.1.341 created 2017]
 
 
EC 2.1.1.382     
Accepted name: methoxylated aromatic compound—corrinoid protein Co-methyltransferase
Reaction: a methoxylated aromatic compound + a [Co(I) methoxylated-aromatic-compound-specific corrinoid protein] = a [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein] + a phenol
Other name(s): mtoB (gene name); mtvB (gene name); vdmB (gene name)
Systematic name: methoxylated aromatic compound:cobamide Co-methyltransferase
Comments: This entry stands for a family of enzymes that have been characterized from acetogenic bacteria and archaeal species. Different members of this family have different substrate specificity. In the methanogenic archaeon Methermicoccus shengliensis the enzyme participates in methanogenesis from methoxylated aromatic compounds, while in acetogenic bacteria and in non-methanogenic archaea it participates in methoxydotrophic growth. Most of the enzymes have a wide specificity and were shown to act on a large number of methoxylated aromatic compounds, carrying a methoxy group at positions 2, 3 or 4 of the aromatic ring. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state; during methylation the cobalt is oxidized to the Co(III) state.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kaufmann, F., Wohlfarth, G. and Diekert, G. O-demethylase from Acetobacterium dehalogenans—substrate specificity and function of the participating proteins. Eur. J. Biochem. 253 (1998) 706–711. [DOI] [PMID: 9654069]
2.  Engelmann, T., Kaufmann, F. and Diekert, G. Isolation and characterization of a veratrol:corrinoid protein methyl transferase from Acetobacterium dehalogenans. Arch. Microbiol. 175 (2001) 376–383. [DOI] [PMID: 11409548]
3.  Naidu, D. and Ragsdale, S.W. Characterization of a three-component vanillate O-demethylase from Moorella thermoacetica. J. Bacteriol. 183 (2001) 3276–3281. [DOI] [PMID: 11344134]
4.  Pierce, E., Xie, G., Barabote, R.D., Saunders, E., Han, C.S., Detter, J.C., Richardson, P., Brettin, T.S., Das, A., Ljungdahl, L.G. and Ragsdale, S.W. The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum). Environ. Microbiol. 10 (2008) 2550–2573. [DOI] [PMID: 18631365]
5.  Kurth, J.M., Nobu, M.K., Tamaki, H., de Jonge, N., Berger, S., Jetten, M.SM., Yamamoto, K., Mayumi, D., Sakata, S., Bai, L., Cheng, L., Nielsen, J.L., Kamagata, Y., Wagner, T. and Welte, C.U. Methanogenic archaea use a bacteria-like methyltransferase system to demethoxylate aromatic compounds. ISME J. 15 (2021) 3549–3565. [DOI] [PMID: 34145392]
6.  Welte, C.U., de Graaf, R., Dalcin Martins, P., Jansen, R.S., Jetten, M.SM. and Kurth, J.M. A novel methoxydotrophic metabolism discovered in the hyperthermophilic archaeon Archaeoglobus fulgidus. Environ. Microbiol. 23 (2021) 4017–4033. [DOI] [PMID: 33913565]
[EC 2.1.1.382 created 2022]
 
 
EC 2.1.1.385     
Accepted name: [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein]—tetrahydrofolate methyltransferase
Reaction: a [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein] + tetrahydrofolate = N5-methyltetrahydrofolate + a [Co(I) methoxylated-aromatic-compound-specific corrinoid protein]
Other name(s): mtvA (gene name)
Systematic name: [methylated methoxylated-aromatic-compound-specific corrinoid protein]:tetrahydrofolaten methyltransferase
Comments: The enzyme, found in acetogenic bacteria, participates in a pathway for the degradation of methoxylated aromatic compounds (methoxydotrophic growth). The enzyme catalyses the transfer of a methyl group bound to the cobalt cofactor of a dedicated corrinoid protein (MtvC) to tetrahydrofolate. cf. EC 2.1.1.384, [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein]—tetrahydromethanopterin methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kaufmann, F., Wohlfarth, G. and Diekert, G. O-demethylase from Acetobacterium dehalogenans—substrate specificity and function of the participating proteins. Eur. J. Biochem. 253 (1998) 706–711. [DOI] [PMID: 9654069]
2.  Naidu, D. and Ragsdale, S.W. Characterization of a three-component vanillate O-demethylase from Moorella thermoacetica. J. Bacteriol. 183 (2001) 3276–3281. [DOI] [PMID: 11344134]
3.  Pierce, E., Xie, G., Barabote, R.D., Saunders, E., Han, C.S., Detter, J.C., Richardson, P., Brettin, T.S., Das, A., Ljungdahl, L.G. and Ragsdale, S.W. The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum). Environ. Microbiol. 10 (2008) 2550–2573. [DOI] [PMID: 18631365]
[EC 2.1.1.385 created 2022]
 
 
EC 2.4.1.136     
Accepted name: gallate 1-β-glucosyltransferase
Reaction: UDP-glucose + gallate = UDP + 1-galloyl-β-D-glucose
Other name(s): UDP-glucose—vanillate 1-glucosyltransferase; UDPglucose:vanillate 1-O-glucosyltransferase; UDPglucose:gallate glucosyltransferase
Systematic name: UDP-glucose:gallate β-D-glucosyltransferase
Comments: A number of substituted benzoic acids and, more slowly, cinnamic acids, can act as acceptors. Vanillin is the best acceptor investigated.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 89700-30-1
References:
1.  Gross, G.G. Synthesis of β-glucogallin from UDP-glucose and gallic acid by an enzyme preparation from oak leaves. FEBS Lett. 148 (1982) 67–70.
2.  Gross, G.G. Partial-purification and properties of UDP-glucose-vanillate 1-O-glucosyl transferase from oak leaves. Phytochemistry 22 (1983) 2179–2182.
[EC 2.4.1.136 created 1984]
 
 
EC 2.4.1.300     
Accepted name: cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)
Reaction: 1-O-vanilloyl-β-D-glucose + cyanidin 3-O-β-D-glucoside = vanillate + cyanidin 3,7-di-O-β-D-glucoside
For diagram of anthocyanidin glucoside biosynthesis, click here
Glossary: vanillate = 4-hydroxy-3-methoxybenzoate
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
Other name(s): AA7GT
Systematic name: 1-O-vanilloyl-β-D-glucose:cyanidin-3-O-β-D-glucoside 7-O-β-D-glucosyltransferase
Comments: Isolated from the plant Delphinium grandiflorum (delphinium). Also acts on other anthocyanidins and with other acyl-glucose derivatives.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Matsuba, Y., Sasaki, N., Tera, M., Okamura, M., Abe, Y., Okamoto, E., Nakamura, H., Funabashi, H., Takatsu, M., Saito, M., Matsuoka, H., Nagasawa, K. and Ozeki, Y. A novel glucosylation reaction on anthocyanins catalyzed by acyl-glucose-dependent glucosyltransferase in the petals of carnation and delphinium. Plant Cell 22 (2010) 3374–3389. [DOI] [PMID: 20971893]
[EC 2.4.1.300 created 2013]
 
 
EC 4.1.2.41      
Transferred entry: vanillin synthase. Now included with EC 4.1.2.61, feruloyl-CoA hydratase/lyase
[EC 4.1.2.41 created 2000, deleted 2019]
 
 
EC 4.2.1.83     
Accepted name: 4-oxalomesaconate hydratase
Reaction: 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = (1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate + H2O
For diagram of the protocatechuate 3,4-cleavage pathway, click here
Other name(s): 4-oxalmesaconate hydratase; 4-carboxy-2-oxohexenedioate hydratase; 4-carboxy-2-oxobutane-1,2,4-tricarboxylate 2,3-hydro-lyase; oxalmesaconate hydratase; γ-oxalmesaconate hydratase; 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate 2,3-hydro-lyase; LigJ; GalB
Systematic name: (1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate 1,2-hydro-lyase (2-hydroxy-4-oxobutane-1,2,4-tricarboxylate-forming)
Comments: This enzyme participates in the degradation of 3,4-dihydroxybenzoate (via the meta-cleavage pathway), syringate and 3,4,5-trihydroxybenzoate, catalysing the reaction in the opposite direction [1-3]. It accepts the enol-form of 4-oxalomesaconate, 2-hydroxy-4-carboxy-hexa-2,4-dienedioate [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 85204-95-1
References:
1.  Maruyama, K. Enzymes responsible for degradation of 4-oxalmesaconic acid in Pseudomonas ochraceae. J. Biochem. 93 (1983) 567–574. [PMID: 6841354]
2.  Maruyama, K. Purification and properties of γ-oxalomesaconate hydratase from Pseudomonas ochraceae grown with phthalate. Biochem. Biophys. Res. Commun. 128 (1985) 271–277. [DOI] [PMID: 3985968]
3.  Hara, H., Masai, E., Katayama, Y. and Fukuda, M. The 4-oxalomesaconate hydratase gene, involved in the protocatechuate 4,5-cleavage pathway, is essential to vanillate and syringate degradation in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 182 (2000) 6950–6957. [DOI] [PMID: 11092855]
4.  Nogales, J., Canales, A., Jiménez-Barbero, J., Serra B., Pingarrón, J. M., García, J. L. and Díaz, E. Unravelling the gallic acid degradation pathway in bacteria: the gal cluster from Pseudomonas putida. Mol. Microbiol. 79 (2011) 359–374. [DOI] [PMID: 21219457]
[EC 4.2.1.83 created 1986, modified 2011]
 
 


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