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Literature summary extracted from

  • Ding, W.; Si, M.; Zhang, W.; Zhang, Y.; Chen, C.; Zhang, L.; Lu, Z.; Chen, S.; Shen, X.
    Functional characterization of a vanillin dehydrogenase in Corynebacterium glutamicum (2015), Sci. Rep., 5, 8044 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.67 gene vdh, phylogenetic tree Corynebacterium glutamicum

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.67 C292A site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+, the activity of N157A decreases to10% of the wild-type activity Corynebacterium glutamicum
1.2.1.67 E199A site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+ the activity of E199A decreases to 78% of the wild-type activity Corynebacterium glutamicum
1.2.1.67 E258A site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme Corynebacterium glutamicum
1.2.1.67 K180A site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+, the activity of N157A decreases to10% of the wild-type activity Corynebacterium glutamicum
1.2.1.67 additional information generation of a vdh deletion mutant, which 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 Corynebacterium glutamicum
1.2.1.67 N157A site-directed mutagensis, the mutant shows over 50% reduced activity compared to the wild-type enzyme. In presence of NADP+, the activity of N157A decreases to10% of the wild-type activity Corynebacterium glutamicum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.67 49500
-
 monomer, gel filtration Corynebacterium glutamicum
1.2.1.67 92300
-
 dimer, gel filtration Corynebacterium glutamicum
1.2.1.67 159000
-
 trimer, gel filtration Corynebacterium glutamicum
1.2.1.67 199200
-
 tetramer, gel filtration Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.67 vanillin + NAD+ + H2O Corynebacterium glutamicum
-
 vanillate + NADH + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.67 Corynebacterium glutamicum Q8NMB0
-
-
1.2.1.67 Corynebacterium glutamicum ATCC 13032 Q8NMB0
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.67 3,4-dihydroxybenzaldehyde + NAD+ + H2O
-
 Corynebacterium glutamicum 3,4-dihydroxybenzoate + NADH + 2 H+
-
 ?
1.2.1.67 4-hydroxybenzaldehyde + NAD+ + H2O
-
 Corynebacterium glutamicum 4-hydroxybenzoate + NADH + 2 H+
-
 ?
1.2.1.67 4-hydroxybenzaldehyde + NAD+ + H2O
-
 Corynebacterium glutamicum ATCC 13032 4-hydroxybenzoate + NADH + 2 H+
-
 ?
1.2.1.67 benzaldehyde + NAD+ + H2O
-
 Corynebacterium glutamicum benzoate + NADH + 2 H+
-
 ?
1.2.1.67 benzaldehyde + NAD+ + H2O
-
 Corynebacterium glutamicum ATCC 13032 benzoate + NADH + 2 H+
-
 ?
1.2.1.67 cinnamaldehyde + NAD+ + H2O
-
 Corynebacterium glutamicum cinnamate + NADH + 2 H+
-
 ?
1.2.1.67 cinnamaldehyde + NAD+ + H2O
-
 Corynebacterium glutamicum ATCC 13032 cinnamate + NADH + 2 H+
-
 ?
1.2.1.67 additional information product dentification by mass spectroscopic analysis Corynebacterium glutamicum ?
-
 ?
1.2.1.67 additional information product dentification by mass spectroscopic analysis Corynebacterium glutamicum ATCC 13032 ?
-
 ?
1.2.1.67 o-phthaldialdehyde + NAD+ + H2O
-
 Corynebacterium glutamicum ? + NADH + 2 H+
-
 ?
1.2.1.67 syringaldehyde + NAD+ + H2O
-
 Corynebacterium glutamicum syringate + NADH + H+
-
 ?
1.2.1.67 syringaldehyde + NAD+ + H2O
-
 Corynebacterium glutamicum ATCC 13032 syringate + NADH + H+
-
 ?
1.2.1.67 vanillin + NAD+ + H2O
-
 Corynebacterium glutamicum vanillate + NADH + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.67 More VDHATCC13032 exists as tetramer, trimer and dimer Corynebacterium glutamicum
1.2.1.67 oligomer x * 51000, SDS-PAGE Corynebacterium glutamicum

Synonyms

EC Number Synonyms Comment Organism
1.2.1.67 VDH
-
 Corynebacterium glutamicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.67 30
-
-
 Corynebacterium glutamicum

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.2.1.67 5 60 activity range, profile overview Corynebacterium glutamicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.67 7
-
-
 Corynebacterium glutamicum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.2.1.67 3 9.5 activity range, profile overview Corynebacterium glutamicum

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.67 additional information the enzyme can utilize NAD+ and NADP+ as coenzymes with similar efficiency and shows no obvious difference toward NAD+ and NADP+ Corynebacterium glutamicum
1.2.1.67 NAD+
-
 Corynebacterium glutamicum
1.2.1.67 NADP+
-
 Corynebacterium glutamicum

General Information

EC Number General Information Comment Organism
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 Corynebacterium glutamicum
1.2.1.67 additional information 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 Corynebacterium glutamicum
1.2.1.67 physiological function vanillin dehydrogenase is a crucial enzyme involved in the degradation of lignin-derived phenylpropanoids, such as vanillin, vanillate, caffeate, p-coumarate, and cinnamate Corynebacterium glutamicum