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Information on EC 1.1.1.194 - coniferyl-alcohol dehydrogenase
for references in articles please use BRENDA:EC1.1.1.194
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.194 coniferyl-alcohol dehydrogenase
IUBMB Comments
Specific for coniferyl alcohol; does not act on cinnamyl alcohol, 4-coumaryl alcohol or sinapyl alcohol.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
showSynonyms
coniferyl alcohol dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CAD
coniferyl alcohol dehydrogenase
CAD
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coniferyl alcohol + NADP+ = coniferyl aldehyde + NADPH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
capsiconiate biosynthesis, phenylpropanoid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
coniferyl-alcohol:NADP+ oxidoreductase
Specific for coniferyl alcohol; does not act on cinnamyl alcohol, 4-coumaryl alcohol or sinapyl alcohol.
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CAS REGISTRY NUMBER
COMMENTARY
37250-27-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
r
sinapyl alcohol + NADP+
sinapyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
sinapyl aldehyde + NADPH + H+
sinapyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
coniferyl alcohol
-
the enzyme is inhibited by an excess of coniferyl alcohol from 0.017 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (142 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, hydroxyapatite column chromatography and Sephadex G-100 gel filtration
-
ammonium sulfate precipitation, Resource PHE column chromatography, and Mono Q Superdex 200 column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene calA, co-expression of the enzyme from strain HR199 with Rhodococcus sp.strain HR199 coniferyl aldehyde dehydrogenase, and Penicillium simplicissimus strain CBS vanillyl alcohol oxidase in the deficient Rhodococcus opacus strain PD630, subcloning in Escherichia coli srain XL 1-Blue
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
nutrition
synthesis
biotechnology
-
the recombinant Rhodococcus opacus strain PD630, expressing the coniferyl alcohol dehydrogenase from Rhodococcus sp. strain HR199, together with the coniferyl aldehyde dehydrogenase, and the vanillyl alcohol oxidase, the latter from Penicillium simplicissimus strain CBS, is able to produce vanillin from ferulic acid and eugenol
biotechnology
Rhodococcus sp. HR199
-
the recombinant Rhodococcus opacus strain PD630, expressing the coniferyl alcohol dehydrogenase from Rhodococcus sp. strain HR199, together with the coniferyl aldehyde dehydrogenase, and the vanillyl alcohol oxidase, the latter from Penicillium simplicissimus strain CBS, is able to produce vanillin from ferulic acid and eugenol
-
nutrition
-
the recombinant Rhodococcus opacus strain PD630, expressing the coniferyl alcohol dehydrogenase from Rhodococcus sp. strain HR199, together with the coniferyl aldehyde dehydrogenase, and the vanillyl alcohol oxidase, the latter from Penicillium simplicissimus strain CBS, is able to produce vanillin from ferulic acid and eugenol
nutrition
Rhodococcus sp. HR199
-
the recombinant Rhodococcus opacus strain PD630, expressing the coniferyl alcohol dehydrogenase from Rhodococcus sp. strain HR199, together with the coniferyl aldehyde dehydrogenase, and the vanillyl alcohol oxidase, the latter from Penicillium simplicissimus strain CBS, is able to produce vanillin from ferulic acid and eugenol
-
synthesis
-
the recombinant Rhodococcus opacus strain PD630, expressing the coniferyl alcohol dehydrogenase from Rhodococcus sp. strain HR199, together with the coniferyl aldehyde dehydrogenase, and the vanillyl alcohol oxidase, the latter from Penicillium simplicissimus strain CBS, is able to produce vanillin from ferulic acid and eugenol
synthesis
Rhodococcus sp. HR199
-
the recombinant Rhodococcus opacus strain PD630, expressing the coniferyl alcohol dehydrogenase from Rhodococcus sp. strain HR199, together with the coniferyl aldehyde dehydrogenase, and the vanillyl alcohol oxidase, the latter from Penicillium simplicissimus strain CBS, is able to produce vanillin from ferulic acid and eugenol
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wyrambik, D.; Grisebach, H.
Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures
Eur. J. Biochem.
59
9-15
1975
Glycine max
brenda
Dalkin, K.; Edwards, R.; Edington, B.; Dixon, R.A.
Stress responses in alfalfa (Medicago sativa L.). I. Induction of phenylpropanoid biosynthesis and hydrolytic enzymes in elicitor-treated cell suspension cultures
Plant Physiol.
92
440-446
1990
Medicago sativa
brenda
Ranjeva, R.; Boudet, A.M.; Harada, H.; Marigo, G.
Phenolic metabolism in petunia tissues. I. Characteristic responses of enzymes involved in different steps of polyphenol synthesis to different hormonal influences
Biochim. Biophys. Acta
399
23-30
1975
Petunia x hybrida
brenda
Gross, G.G.; Stckigt, J.; Mansell, R.L.; Zenk, M.H.
Three novel enzymes involved in the reduction of ferulic acid to coniferyl alcohol in higher plants: ferulate:CoA Ligase, feruloyl-CoA reductase and coniferyl alcohol oxidoreductase
FEBS Lett.
31
283-286
1973
Salix alba
-
brenda
Sauter, M.; Kende, H.
Levels of beta-glucan and lignin in elongating internodes of deepwater rice
Plant Cell Physiol.
33
1089-1097
1992
Oryza sativa
-
brenda
Mansell, Richard L.; Barbel, Gareth R.; Zenk, Meinhart H.
Multiple forms and specificity of coniferyl alcohol dehydrogenase from cambial regions of higher plants
Phytochemistry
15
1849-1853
1976
Acer rubrum, Medicago sativa, Metasequoia glyptostroboides, Pinus palustris, Prunus padus, Salix purpurea, Schinus terebinthifolia, Zea mays
-
brenda
Plaggenborg, R.; Overhage, J.; Loos, A.; Archer, J.A.; Lessard, P.; Sinskey, A.J.; Steinbuechel, A.; Priefert, H.
Potential of Rhodococcus strains for biotechnological vanillin production from ferulic acid and eugenol
Appl. Microbiol. Biotechnol.
72
745-755
2006
Rhodococcus sp., Rhodococcus sp. HR199
brenda
Nishimura, M.
Molecular cloning and expression of the Streptomyces coniferyl alcohol dehydrogenase gene in Escherichia coli
Protein Expr. Purif.
89
109-115
2013
Streptomyces sp. (M5AJW4)
brenda
Alarcon, B.; de Armas, R.; Vicente, C.; Legaz, M.
Inhibition by substrates of a coniferyl alcohol dehydrogenase purified from sugarcane stalks
Curr. Enzyme Inhib.
15
206-214
2019
Saccharum officinarum
-
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.194)
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