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Literature summary extracted from

  • Fleige, C.; Hansen, G.; Kroll, J.; Steinbuechel, A.
    Investigation of the Amycolatopsis sp. strain ATCC 39116 vanillin dehydrogenase and its impact on the biotechnical production of vanillin (2013), Appl. Environ. Microbiol., 79, 81-90.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.2.1.67 biotechnology Amycolatopsis sp. ATCC 39116 vdh mutant represents an optimized and industrially applicable platform for biotechnological production of natural vanillin Amycolatopsis sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.67 vdh gene cloned into pET23a(+)vector heterologously expressed with C-terminal His6-tag in Escherichia coli BL21(DE3) cells Amycolatopsis sp.

General Stability

EC Number General Stability Organism
1.2.1.67 after storage at 4°C for 24 h, the enzyme exhibits 86% of its former activity Amycolatopsis sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.67 54000
-
 SDS-PAGE Amycolatopsis sp.

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.67 Amycolatopsis sp. K9UV87
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.67 purified to apparent electrophoretic homogeneity using His SpinTrap columns Amycolatopsis sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.1.67 additional information
-
 no VDH activity detectable in cells that are cultivated with gluconate as the sole carbon source Amycolatopsis sp.
1.2.1.67 0.025
-
 crude extract, when cells are previously cultivated with vanillin as the carbon source, pH 7.1 and 30°C Amycolatopsis sp.
1.2.1.67 0.072
-
 purified recombinant protein, low activity due to loss of activity during purification, pH 7.1 and 30°C Amycolatopsis sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.67 benzaldehyde + NAD+ + H2O 66% activity in comparison to vanillin Amycolatopsis sp. benzoate + NADH + 2 H+
-
 ?
1.2.1.67 cinnamaldehyde + NAD+ + H2O
-
 Amycolatopsis sp. cinnamate + NADH + 2 H+
-
 ?
1.2.1.67 coniferylaldehyde + NAD+ + H2O
-
 Amycolatopsis sp. coniferic acid + NADH + 2 H+
-
 ?
1.2.1.67 additional information vdh deletion mutant loses its ability to grow on vanillin and does not show vanillin dehydrogenase activity, 2.3fold higher vanillin concentration in vdh mutants observed when ferulic acid is provided for biotransformation in a cultivation experiment Amycolatopsis sp. ?
-
 ?
1.2.1.67 vanillin + NAD+ + H2O no enzyme activity observed in the absence of NAD+, no oxidation of vanillin detectable when NADP+ used as cofactor Amycolatopsis sp. vanillate + NADH + 2 H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.67 vanillin dehydrogenase
-
 Amycolatopsis sp.
1.2.1.67 VDH
-
 Amycolatopsis sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.67 44
-
-
 Amycolatopsis sp.

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.2.1.67 15 65
-
 Amycolatopsis sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.67 8
-
-
 Amycolatopsis sp.

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.2.1.67 5 9
-
 Amycolatopsis sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.67 NAD+
-
 Amycolatopsis sp.

General Information

EC Number General Information Comment Organism
1.2.1.67 metabolism Amycolatopsis sp. ATCC 39116 is capable of synthesizing large amounts of vanillin from the natural substrate ferulic acid Amycolatopsis sp.