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, Bmr6, 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 2, dehydrogenase, cinnamyl alcohol, FC1, FLEXIBLE CULM1, More, ScAdh6p

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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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
S212D
-
site-directed mutagenesis and overexpression in Escherichia coli
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