EC Number   |
General Information |
Reference |
|---|
   1.2.1.67 | evolution |
DesV-like ALDHs form a distinct phylogenetic cluster separated from the vanillin dehydrogenase cluster, phylogenetic analyis |
743835 |
| 1.2.1.67 | malfunction |
a gene vdh deletion mutant of Amycolatopsis sp. strain ATCC 39116 shows increased levels of accumulated vanillin |
-, 741700 |
| 1.2.1.67 | malfunction |
disruption of desV in SYK-6 results in a significant reduction in growth on syringaldehyde and in syringaldehyde oxidation activity. A desV-ligV double mutant almost completely loses its ability to grow on syringaldehyde. Purified DesV shows similar kcat/Km values for syringaldehyde and vanillin, whereas LigV substantially prefers vanillin over syringaldehyde |
743835 |
| 1.2.1.67 | malfunction |
the vdh deletion mutant partially loses its ability to grow on vanillin, indicating the presence of alternative VDH(s) in Corynebacterium glutamicum. When complemented with plasmid pXMJ19-vdhATCC13032, the growth ability of the mutant strain can be restored close to that of the wild type. The wild type, the DELTAvdhATCC13032 mutant and the complementary strain shows no difference when grown in p-cresol, cinnamyl aldehyde and syringaldehyde |
-, 743803 |
| 1.2.1.67 | metabolism |
Amycolatopsis sp. ATCC 39116 is capable of synthesizing large amounts of vanillin from the natural substrate ferulic acid |
724040 |
| 1.2.1.67 | metabolism |
enzyme is involved in lignin degradation because one degradation product of lignin is vanillin |
724018 |
| 1.2.1.67 | metabolism |
in strain 3NA, ferulic acid is converted to a substance identified as 4-vinylguaiacol (2-methoxy-4-vinylphenol), and vanillin is converted to ca. 97% guaiacol and 3 % vanillyl alcohol, whereas vanillic acid is completely converted to guaiacol. Vanillin is converted to guaiacol, forming vanillic acid as an intermediate product |
-, 741714 |
| 1.2.1.67 | more |
enzyme molecular modeling, dimeric model construction using the structure of ALDH domains of Geobacter sulfurreducens PutA, PDB ID 4NMB, for the enzyme dimer and sheep liver class 1 aldehyde dehydrogenase structure, 1BXS, as the template fo rthe tetramer. molecularmodelling of Cd36_03230p predicts that it has a similar fold to other aldehyde dehydrogenases |
-, 743782 |
| 1.2.1.67 | more |
residues E258 and C292 are identified as the candidate conserved catalytic residues whereas N157, K180 and E199 are identified as the candidate cofactor interactive sites in VDHATCC13032, all residues are important for enzyme activity |
-, 743803 |
| 1.2.1.67 | physiological function |
enzyme DesV plays a major role in syringaldehyde catabolism |
743835 |
