Information on EC 1.2.1.68 - coniferyl-aldehyde dehydrogenase:

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The lowest common taxonomy group for this enzyme is: Proteobacteria

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EC NUMBERCOMMENTARY
1.2.1.68-

RECOMMENDED NAMEGeneOntology No.
coniferyl-aldehyde dehydrogenaseGO:0050269

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
coniferyl aldehyde + H2O + NAD(P)+ = ferulate + NAD(P)H + 2 H+
show the reaction diagram
----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
oxidation----
redox reaction----
reduction----

PATHWAYKEGG LinkMetaCyc Link
ferulate and sinapate biosynthesis-PWY-5168

SYSTEMATIC NAMEIUBMB Comments
coniferyl aldehyde:NAD(P)+ oxidoreductaseAlso oxidizes other aromatic aldehydes, but not aliphatic aldehydes.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
CALDHPseudomonas sp.--288325
coniferyl aldehyde dehydrogenasePseudomonas sp.Q86447-654264

CAS REGISTRY NUMBERCOMMENTARY
208540-41-4-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Pseudomonas sp.strain HR199288325--Manually annotated by BRENDA team
Pseudomonas sp.strain HR199654264Q86447SwissProtManually annotated by BRENDA team
Pseudomonas sp.strain HR199654275O86447UniprotManually annotated by BRENDA team
Pseudomonas sp. HR199strain HR199288325--Manually annotated by BRENDA team
Pseudomonas sp. HR199strain HR199654264O86447SwissProtManually annotated by BRENDA team
Pseudomonas sp. HR199strain HR199654275O86447-Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate
LITERATURE/
Substrate
COMMENTARY/
Product
LITERATURE/
Product
Reversibility
r=reversible
ir=irreversible
?=not specified
coniferyl aldehyde + H2O + NAD+ferulate + NADH
show the reaction diagram
Pseudomonas sp.Q86447-654264--?
coniferyl aldehyde + H2O + NAD+ferulate + NADH
show the reaction diagram
Pseudomonas sp.-involved in the eugenol catabolism288325-288325?
coniferyl aldehyde + H2O + NAD+ferulate + NADH
show the reaction diagram
Pseudomonas sp.Q86447involved in eugenol catabolism654264--?
coniferyl aldehyde + H2O + NADP+ferulate + NADPH
show the reaction diagram
Pseudomonas sp.-4.3% of the rate compared to NAD+ as electron acceptor288325-288325?

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)
COMMENTARY PRODUCTLITERATURE
(Product)
coniferyl aldehyde + H2O + NAD+ferulate + NADH
show the reaction diagram
Pseudomonas sp.-involved in the eugenol catabolism288325-288325
coniferyl aldehyde + H2O + NAD+ferulate + NADH
show the reaction diagram
Pseudomonas sp.Q86447involved in eugenol catabolism654264--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
NAD+Pseudomonas sp.--288325 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
No entries in this field

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0070.012coniferyl aldehydePseudomonas sp.--288325 2D-image
0.334-NAD+Pseudomonas sp.--288325 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
36.54-Pseudomonas sp.--288325

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
8.8-Pseudomonas sp.--288325

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
26-Pseudomonas sp.--288325

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
cell culturePseudomonas sp.-induction of enzyme synthesis by growth in eugenol-containing media288325Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
86000-Pseudomonas sp.-gel filtration288325

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
dimerPseudomonas sp.-alpha2, 2 * 49500, SDS-PAGE288325

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
8.8-Pseudomonas sp.-very unstable288325

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
26-Pseudomonas sp.-rapid decrease of activity at higher temperatures288325

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
to homogeneity, chromatography techniquesPseudomonas sp.-288325

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
additional informationPseudomonas sp.O86447expression of the vaoA gene from Penicillium simplicissimum CBS 170.90, encoding vanillyl alcohol oxidase, which also catalyzes the conversion of eugenol to coniferyl alcohol, is expressed in Escherichia coli XL-1 Blue under the control of the lac promoter, together with the genes calA and calB, encoding coniferyl alcohol dehydrogenase and coniferyl aldehyde dehydrogenase of Pseudomonas sp. strain HR199, respectively654275

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
biotechnologyPseudomonas sp.Q86447biotransformation of eugenol to ferulic acid by a recombinant strain of Ralstonia eutropha H16. The gene calB, encoding coniferyl aldehyde dehydrogenase, and ehyAB and calA encoding eugenol hydroxylase and coniferyl alcohol dehydrogenase, respectively, are amplified and combined to construct a catabolic gene cassette. This gene cassette is cloned in the broad-host-range vector pBBR1-JO2 and transferred to Ralstonia eutropha H16. A recombinant strain of Ralstonia eutropha H16 harboring this plasmid expresses functionally active eugenol hydroxylase, coniferyl alcohol dehydrogenase, and coniferyl aldehyde dehydrogenase. Cells of Ralstonia eutropha H16 from the late-exponential growth phase are used asa biocatalysts for the biotransformation of eugenol to ferulic acid. A maximum conversion rate of 2.9 mM of eugenol per h per liter of culture is achieved with a yield of 93.8 mol% of ferulic acid from eugenol within 20 h, without further optimization654264
biotechnologyPseudomonas sp.O86447highly efficient two-step biotransformation of eugenol to ferulic acid and further conversion to vanillin in recombinant strains of Escherichia coli. Maximum production rate for ferulic acid at large scale is 14.4 mM per h per liter of culture, yield of 93.3% with respect to the added amount of eugenol654275
nutritionPseudomonas sp.-production of vanillin288325

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
288325Achterholt, S.; Priefert, H.; Steinbuchel, A.Purification and characterization of the coniferyl aldehyde dehydrogenase from Pseudomonas sp. strain HR199 and molecular characterization of the geneJ. Bacteriol.1804387-43911998Pseudomonas sp. PubMed
654264Overhage, J.; Steinbuchel, A.; Priefert, H.Biotransformation of eugenol to ferulic acid by a recombinant strain of Ralstonia eutropha H16Appl. Environ. Microbiol.684315-43212002Pseudomonas sp. PubMed
654275Overhage, J.; Steinbuchel, A.; Priefert, H.Highly efficient biotransformation of eugenol to ferulic acid and further conversion to vanillin in recombinant strains of Escherichia coliAppl. Environ. Microbiol.696569-65762003Pseudomonas sp. PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.68)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)