Vanillin dehydrogenase
Vanillin dehydrogenase | ||
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Mass / length primary structure | 482 amino acids (in Pseudomonas putida strain KT2440) | |
Cofactor | NAD + | |
Identifier | ||
External IDs |
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Enzyme classification | ||
EC, category | 1.2.1.67 , oxidoreductase | |
Substrate | Vanillin, H 2 O | |
Products | Vanillic acid, 2 H + | |
Occurrence | ||
Parent taxon | Pseudomonas |
A vanillin dehydrogenase (VDH, EC 1.2.1.67 ) is an enzyme which catalyzes the reaction of vanillin to vanillic acid catalyzed. Dehydrogenase belongs to the family of oxidoreductases .
NAD + , which is reduced to NADH, is required as a cofactor for the reaction :
The enzyme has been detected in Pseudomonas putida and Pseudomonas fluorescens , among others . There, vanillin is an intermediate product in the breakdown of ferulic acid to protocatechuic acid , which is then further metabolized after ring cleavage.
The absence of the cofactor NAD + reduces the enzymatic activity in P. fluorescens .
Homologous enzymes have also been found in Burkholderia species and generally belong to the aldehyde dehydrogenases .
Individual evidence
- ↑ a b A. Narbad, MJ Gasson: Metabolism of ferulic acid via vanillin using a novel CoA-dependent pathway in a newly-isolated strain of Pseudomonas fluorescens. In: Microbiology. 144 (Pt 5), 1998, pp. 1397-1405. PMID 9611814 ; ( PDF , free full text access, English)
- ↑ R. Plaggenborg, J. Overhage, A. Steinbüchel, H. Prichert: Functional analyzes of genes involved in the metabolism of ferulic acid in Pseudomonas putida KT2440. In: Appl Microbiol Biotechnol. 61 (5-6), 2003, pp. 528-535. PMID 12764569 ; doi: 10.1007 / s00253-003-1260-4 .
- ↑ Homologues at OMA