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Literature summary for 1.2.1.30 extracted from

  • Venkitasubramanian, P.; Daniels, L.; Das, S.; Lamm, A.S.; Rosazza, J.P.
    Aldehyde oxidoreductase as a biocatalyst: Reductions of vanillic acid (2008), Enzyme Microb. Technol., 42, 130-137.
    View publication on PubMed
Search for more literature for 1.2.1.30

Activating Compound

Activating Compound Comment Organism Structure
additional information levels of recombinant Car and Gdh are slightly higher when cultures are grown without chloramphenicol Nocardia iowensis

Application

Application Comment Organism
industry vanillic acid reduction in Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.85 cells containing car, npt and gdh is complete in 6 h, and is faster than in cells containing only car and/or npt. The availability of Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.85 expressing holo-Car and Gdh provides a means of generating a range of value-added aldehydes or alcohols of importance in pharmaceutical, food and agricultural industries. Uses of directed evolution and related mutant generating processes, may enable a Car-system with broader substrate specificities and one that is capable of achieving much higher product yields Nocardia iowensis

Cloned(Commentary)

Cloned (Comment) Organism
plasmids pHAT305(Placcar), pPV2.83(Placcar Placnpt), pPV2.84(Placcar Placgdh) or pPV2.85(Placcar Plac npt gdh) expressed in Escherichia coli BL21-CodonPlus(DE3)-RP cells Nocardia iowensis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Nocardia iowensis

Organism

Organism UniProt Comment Textmining
Nocardia iowensis Q6RKB1
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.36
-
 recombinant Car expressed in Escherichia coli BL21-CodonPlus(DE3)-RP cells cultured in LB medium with ampicillin, at 16 h Nocardia iowensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-ketoglutaric acid + NADPH + ATP
-
 Nocardia iowensis ? + NADP+ + AMP + phosphate
-
 ?
benzoic acid + NADPH + H+ + ATP
-
 Nocardia iowensis benzaldehyde + benzyl alcohol + NADP+ + AMP + diphosphate
-
 ?
cis-aconitic acid + NADPH + ATP
-
 Nocardia iowensis ? + NADP+ + AMP + phosphate
-
 ?
citric acid + NADPH + ATP
-
 Nocardia iowensis ? + NADP+ + AMP + phosphate
-
 ?
D-malic acid + NADPH + ATP
-
 Nocardia iowensis ? + NADP+ + AMP + phosphate
-
 ?
DL-malic acid + NADPH + ATP
-
 Nocardia iowensis ? + NADP+ + AMP + phosphate
-
 ?
ferulic acid + NADPH + H+ + ATP not completely reduced Nocardia iowensis ferulic acid + coniferyl aldehyde + coniferyl alcohol + NADP+ + AMP + diphosphate
-
 ?
L-malic acid + NADPH + ATP
-
 Nocardia iowensis ? + NADP+ + AMP + phosphate
-
 ?
additional information pyruvic, isocitric acid, fumaric acid and maleic acid are not substrates for the enzyme Nocardia iowensis ?
-
 ?
trans-aconitic acid + NADPH + ATP
-
 Nocardia iowensis ? + NADP+ + AMP + phosphate
-
 ?
vanillic acid + NADPH + H+ + ATP
-
 Nocardia iowensis vanillin + NADP+ + AMP + diphosphate
-
 ?

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Nocardia iowensis
NADPH
-
 Nocardia iowensis