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1.1.1.203: uronate dehydrogenase

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

Word Map on EC 1.1.1.203

Reaction

beta-D-galacturonate
+
NAD+
=
D-galactaro-1,5-lactone
+
NADH
+
H+

Synonyms

Atu3143, CsUDH, D-galacturonate (uronate) dehydrogenase, D-GalUA oxidoreductase, EC 1.2.1.35, galacturonate acid reductase, galacturonate oxidoreductase, GalUR, Gor, PfUDH, PmUDH, PnUDH, poly-d-galacturonase, PSPTO_1053, PsUDH, Udh, uronate dehydrogenase, uronate:NAD-oxidoreductase, uronic acid dehydrogenase

ECTree

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

Engineering

Engineering on EC 1.1.1.203 - uronate dehydrogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A39P
-
the mutant shows 103.5% activity compared to the wild type enzyme
A39P/H234K
-
the mutant shows 165.7% activity compared to the wild type enzyme
A39P/H99Y
-
the mutant shows 146.8% activity compared to the wild type enzyme
A39P/H99Y/H234K
-
the triple mutant shows 247.6% activity compared to the wild type enzyme, a 400fold improvement in half-life at 59°C, and a 5°C improvement in T50 (10 min) value
A41P/H101N/H236K
-
the mutant shows 52.3% catalytic efficiency as compared to the wild type enzyme
A41P/H101N/H236R
-
the mutant shows 59.3% catalytic efficiency as compared to the wild type enzyme
A41P/H101Y/H236K
-
the mutant shows 58.4% catalytic efficiency, higher kinetic and thermodynamic stability with a T50 value of 62.2°C after 15 min (3.2°C improvement) as compared to the wild type enzyme
A41P/H101Y/H236R
-
the mutant shows 56% catalytic efficiency as compared to the wild type enzyme
A41P/H236K
-
the mutant shows 62.7% catalytic efficiency as compared to the wild type enzyme
D34S
the mutant shows a high selectivity of D-galacturonic acid and its substrate intermediates for D-galactaric acid production
H101N/H236K
-
the mutant shows 48.8% catalytic efficiency as compared to the wild type enzyme
H101Y/H236K
-
the mutant shows 40.8% catalytic efficiency as compared to the wild type enzyme
H234K
-
the mutant shows 129.4% activity compared to the wild type enzyme
H236K
-
the mutant shows 34% catalytic efficiency as compared to the wild type enzyme
H99Y
-
the mutant shows 109.6% activity compared to the wild type enzyme
H99Y/H234K
-
the mutant shows 175.4% activity compared to the wild type enzyme
N112E
the mutant shows a high selectivity of D-galacturonic acid and its substrate intermediates for D-galactaric acid production
Q14F
the mutant shows a high binding affinity to D-glucuronic acid and its substrate intermediates such as D-glucaro-1,4-lactone and D-glucaro-1,5-lactone. The mutant exhibits a low binding affinity to the substrate and cofactor required for D-galactaric acid production
S165E
the mutant shows a high selectivity of D-galacturonic acid and its substrate intermediates for D-galactaric acid production
S36L
the mutant shows a high binding affinity to D-glucuronic acid and its substrate intermediates such as D-glucaro-1,4-lactone and D-glucaro-1,5-lactone. The mutant exhibits a low binding affinity to the substrate and cofactor required for D-galactaric acid production
S75T
the mutant shows a high binding affinity to D-glucuronic acid and its substrate intermediates such as D-glucaro-1,4-lactone and D-glucaro-1,5-lactone. The mutant exhibits a low binding affinity to the substrate and cofactor required for D-galactaric acid production
Y136A
inactive. Crystal structure shows changes in the position of residues Ile74 and Ser75. This probably alters the binding of the nicotinamide end of NAD+
D34S
-
the mutant shows a high selectivity of D-galacturonic acid and its substrate intermediates for D-galactaric acid production
-
N112E
-
the mutant shows a high selectivity of D-galacturonic acid and its substrate intermediates for D-galactaric acid production
-
Q14F
-
the mutant shows a high binding affinity to D-glucuronic acid and its substrate intermediates such as D-glucaro-1,4-lactone and D-glucaro-1,5-lactone. The mutant exhibits a low binding affinity to the substrate and cofactor required for D-galactaric acid production
-
S165E
-
the mutant shows a high selectivity of D-galacturonic acid and its substrate intermediates for D-galactaric acid production
-
S75T
-
the mutant shows a high binding affinity to D-glucuronic acid and its substrate intermediates such as D-glucaro-1,4-lactone and D-glucaro-1,5-lactone. The mutant exhibits a low binding affinity to the substrate and cofactor required for D-galactaric acid production
-
Y136A
Agrobacterium tumefaciens C58 / ATCC 33970
-
inactive. Crystal structure shows changes in the position of residues Ile74 and Ser75. This probably alters the binding of the nicotinamide end of NAD+
-
A39P
-
the mutant shows 103.5% activity compared to the wild type enzyme
-
A39P/H99Y
-
the mutant shows 146.8% activity compared to the wild type enzyme
-
A39P/H99Y/H234K
-
the triple mutant shows 247.6% activity compared to the wild type enzyme, a 400fold improvement in half-life at 59°C, and a 5°C improvement in T50 (10 min) value
-
H234K
-
the mutant shows 129.4% activity compared to the wild type enzyme
-
H99Y
-
the mutant shows 109.6% activity compared to the wild type enzyme
-
A172V
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
D246N
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
I114T
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
I88L
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
L158A/N159C/I160V
the mutant shows increased catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
M175I
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
N99K/L100H/K102V/P103K/I105V
the mutant shows wild type activity with beta-D-glucuronate and reduced catalytic efficiency with beta-D-galacturonate compared to the wild type enzyme
N99K/L100H/K102V/P103K/I105V/Y116F/T113V/A172V/M175I/D236N
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
Q55R
the mutant shows wild type activity with beta-D-glucuronate and reduced catalytic efficiency with beta-D-galacturonate compared to the wild type enzyme
Q55R/I88L/N99K/L100H/K102V/P103K/I105V/T113V/I114T/Y116F/L158A/N159C/I160V/A172V/M175I/D246N
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
T113V
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
T113V/A172V/D246N
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
T113V/A172V/M175I
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
T113V/A172V/M175I/D236N
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
T113V/M175I/D246N
the mutant shows increased catalytic efficiency with beta-D-glucuronate and decreased catalytic efficiency with beta-D-galacturonate compared to the wild type enzyme
Y116F
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme