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.

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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
ENGINEERING
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
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; 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
additional information