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1.1.1.195: cinnamyl-alcohol dehydrogenase

This is an abbreviated version!
For detailed information about cinnamyl-alcohol dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.195

Reaction

cinnamyl alcohol
+
NADP+
=
cinnamaldehyde
+
NADPH
+
H+

Synonyms

ADH, AdhA, alcohol dehydrogenase, AtCAD4, BdCAD1, Bmr6, Bradi3g06480, brown midrib6, Brown-midrib 1 protein, CAD, CAD 7/8, CAD1, CAD10, CAD11, CAD12, CAD13, CAD14, CAD15, CAD2, CAD3, CAD4, CAD5, CAD6, CAD7, CAD8, CAD9, CADH I, cinnamyl alcohol dehydrogenase, cinnamyl alcohol dehydrogenase 1, cinnamyl alcohol dehydrogenase 12, cinnamyl alcohol dehydrogenase 2, cinnamyl alcohol dehydrogenase 3, cinnamyl alcohol dehydrogenase 4, cinnamyl alcohol dehydrogenase 5, cinnamyl alcohol dehydrogenase 7, cinnamyl alcohol dehydrogenase 9, cinnamyl alcohol dehydrogenase C, cinnamyl alcohol dehydrogenases, CtCAD1, CtCAD2, CtCAD3, dehydrogenase, cinnamyl alcohol, FC1, FLEXIBLE CULM1, HcCAD1, HcCAD2, LlCAD2, LtuCAD1, More, Mt-CAD1, Mt-CAD2, PhCAD1, PhCAD2, PhCAD3, PhCAD4, PtoCAD1, PtoCAD12, PtoCAD2, PtoCAD3, PtoCAD5, PtoCAD6, PtoCAD7, PtoCAD8, PtoCAD9, ScAdh6p, TaCAD12

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.195 cinnamyl-alcohol dehydrogenase

Engineering

Engineering on EC 1.1.1.195 - cinnamyl-alcohol dehydrogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D57A
about 4fold increase in catalytic efficiency
H52A
about 40% decrease in catalytic efficiency
T49A
less than 0.5% of wild-type activity. Thermodynamic data indicate a negative enthalpic change, as well as a significant decrease in binding affinity with NADPH. Residue Thr49 is essential for overall catalytic conversion
G575A/G192D
-
the nucleotide substitution G575A occurs in BdCAD1 of the Bd4179 line, and consequently induces the G192D change in the highly conserved glycine-rich NADPH binding site GLGGVG
S212D
-
site-directed mutagenesis and overexpression in Escherichia coli
F226A
-
site-directed mutagenesis, the mutation leads to an enlarged phenolic binding site resulting in a 4fold increase in activity with sinapaldehyde, which in comparison to the smaller coumaraldehyde and coniferaldehyde substrates is disfavored by wild-type CAD2
K169A
-
site-directed mutagenesis, inactive mutant
S130A
-
site-directed mutagenesis, inactive mutant
Y136F
-
site-directed mutagenesis, the mutation leads to an enlarged phenolic binding site resulting in a 10fold increase in activity with sinapaldehyde, which in comparison to the smaller coumaraldehyde and coniferaldehyde substrates is disfavored by wild-type CAD2
Y136F/F226A
-
site-directed mutagenesis, the mutation leads to an enlarged phenolic binding site resulting in a 10fold increase in activity with sinapaldehyde, which in comparison to the smaller coumaraldehyde and coniferaldehyde substrates is disfavored by wild-type CAD2
Y165A
-
site-directed mutagenesis, inactive mutant
Y165F
-
site-directed mutagenesis, inactive mutant
A278V
the isoform CAD4 mutant shows strongly decreased catalytic efficiency compared to the wild type enzyme
G301F
the isoform CAD4 mutant enzyme displays slightly elevated Km values for 4-coumaryl aldehyde but decreased Km for coniferyl aldehyde compared with those values of wild type. The mutant becomes more dedicated toward sinapyl aldehyde, with substantially decreased efficiency for coniferyl aldehyde compared to the wild type enzyme
L119W
the isoform CAD4 mutant displays a slightly reduced Km value for both 4-coumaryl aldehyde and coniferyl aldehyde compared to the wild type enzyme. The mutant becomes more efficient toward coniferaldehyde due to the very small Km value, with substantially decreased efficiency for both sinapyl aldehyde and 4-coumaryl aldehyde
L119W/G301F
the isoform CAD4 double mutant displays its substrate preference in the order coniferyl aldehyde over 4-coumaryl aldehyde over sinapyl aldehyde, with higher catalytic efficiency than that of wild type enzyme. The mutant displays 10 and 800fold increases in its catalytic efficiency for coniferyl aldehyde and 4-coumaryl aldehyde, respectively, and a 50% decrease in catalytic efficiency for sinapyl aldehyde as compared to the wild type enzyme
Q132Stop
mutation responsible for the bmr6 phenotype. Mutation leads to significant reduction in all three main lignin subunits, H-, G-, and S-lignin of 4.8-, 7.3-, and 17.7fold, respectively, relative to the wild type. Lignin subunits S-indene and G-indene are elevated 9.5- and 8.3fold, respectively, in bmr6 relative to the wild type
W58L
the isoform CAD4 mutant enzyme displays slightly elevated Km values for 4-coumaryl aldehyde but decreased Km for coniferyl aldehyde compared with those values of wild type
Y288P
the isoform CAD4 mutant becomes more dedicated toward sinapyl aldehyde, with substantially decreased efficiency for coniferyl aldehyde compared to the wild type enzyme
Y95V
the isoform CAD4 mutant shows decreased catalytic efficiency compared to the wild type enzyme
additional information