Vanillin dehydrogenase

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Vanillin dehydrogenase
Mass / length primary structure 482 amino acids (in Pseudomonas putida strain KT2440)
Cofactor NAD +
Identifier
External IDs
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 :

Vanillin2.svg+ NAD + + H 2 O + NADH + H + Vanillic acid

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

  1. 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)
  2. 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 .
  3. Homologues at OMA