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Information on EC 1.1.1.194 - coniferyl-alcohol dehydrogenase for references in articles please use BRENDA:EC1.1.1.194Word Map on EC 1.1.1.194
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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coniferyl-alcohol dehydrogenase
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coniferyl alcohol + NADP+ = coniferyl aldehyde + NADPH + H+
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capsiconiate biosynthesis
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phenylpropanoid biosynthesis
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coniferyl-alcohol:NADP+ oxidoreductase
Specific for coniferyl alcohol; does not act on cinnamyl alcohol, 4-coumaryl alcohol or sinapyl alcohol.
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coniferyl alcohol dehydrogenase
coniferyl alcohol dehydrogenase
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coniferyl alcohol dehydrogenase
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coniferyl alcohol dehydrogenase
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L. var. Mandarin
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L. deepwater rice
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gene calA
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gene calA
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UniProt
brenda
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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coniferyl alcohol + NADP+
coniferyl aldehyde + NADPH + H+
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NADP+
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NADPH
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additional information
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no reaction with NAD+ or NADH
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additional information
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no reaction with NAD+ or NADH
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0.28 - 0.83
coniferyl alcohol
0.28
coniferyl alcohol
recombinant enzyme, at pH 8.5 and 40°C
0.83
coniferyl alcohol
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25.8
coniferyl alcohol
recombinant enzyme, at pH 8.5 and 40°C
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93.3
coniferyl alcohol
recombinant enzyme, at pH 8.5 and 40°C
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0.27
cell-free extract, at pH 8.5 and 40°C
10.7
after 40fold purification, at pH 8.5 and 40°C
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9.2
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coniferyl alcohol oxidation
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39000
4 * 39000, SDS-PAGE
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homotetramer
4 * 37845, calculated from amino acid sequence; 4 * 39000, SDS-PAGE
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-20°C, 42 mM 2-mercaptoethanol, 10% ethyleneglycol, several weeks
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ammonium sulfate precipitation, Resource PHE column chromatography, and Mono Q Superdex 200 column chromatography
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expressed in Escherichia coli BL21(DE3) cells
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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biotechnology
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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
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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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nutrition
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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
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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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synthesis
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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
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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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CALA_PSEUH
255
27637
Swiss-Prot
BBE13_ARATH
534
60192
Swiss-Prot
BBE15_ARATH
532
59647
Swiss-Prot
A0A1Y0ND50_9BURK
257
27233
TrEMBL
A0A1Y0N8P1_9BURK
254
27327
TrEMBL
Q88K65_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
350
37782
TrEMBL
A0A1S1NKQ5_9MYCO
263
27430
TrEMBL
A0A1S1NLN1_9MYCO
274
28572
TrEMBL
A0A1D3K041_9PSED
255
27092
TrEMBL
A0A2N7R1Q5_9PSED
272
29447
TrEMBL
A0A2K9ZDE2_RHILE
261
26805
TrEMBL
M5AJW4_9ACTN
362
37845
TrEMBL
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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
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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.; Stöckigt, 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
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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
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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
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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
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