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1.23.5.1: violaxanthin de-epoxidase

This is an abbreviated version!
For detailed information about violaxanthin de-epoxidase, go to the full flat file.

Word Map on EC 1.23.5.1

Reaction

antheraxanthin
+
L-ascorbate
=
zeaxanthin
 +
L-dehydroascorbate
 +
H2O

Synonyms

AhVDE, CsVDE, EC 1.10.99.3, lipocalin-like protein, NPQ1, VDE, Vio de-epoxidase, violaxanthin de-epoxidase, Vx de-epoxidase, ZmVDE1

ECTree

     1 Oxidoreductases
         1.23 Reducing C-O-C group as acceptor
             1.23.5 With a quinone or similar compound as acceptor
                1.23.5.1 violaxanthin de-epoxidase

Engineering

Engineering on EC 1.23.5.1 - violaxanthin de-epoxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C118A
site-directed mutagenesis, inactive mutant
C14A
site-directed mutagenesis, inactive mutant
C21A
site-directed mutagenesis, almost inactive mutant
C249A
site-directed mutagenesis, inactive mutant
C27A
site-directed mutagenesis, inactive mutant
C33A
site-directed mutagenesis, inactive mutant
C37A
site-directed mutagenesis, inactive mutant
C46A
site-directed mutagenesis, inactive mutant
C50A
site-directed mutagenesis, the mutant shows 96.5% reduced activity compared to the wild-type enzyme
C65A
site-directed mutagenesis, the mutant shows 95.3% reduced activity compared to the wild-type enzyme
C72A
site-directed mutagenesis, almost inactive mutant
C7A
site-directed mutagenesis, the mutant shows 14.8% reduced activity compared to the wild-type enzyme
C9A
site-directed mutagenesis, inactive mutant
D117A
D178A
the mutant shows 56% activity compared to the wild type enzyme
D206I
D98L/D117A
D98L/D117A/D206I
D98L/D117A/D206I/H168A
DELTA1-4
-
removal of 4 amino acids from the N-terminal region abolishes all violaxanthin de-epoxidase activity
DELTA258-349
-
71 C-terminal amino acid can be removed without affecting activity
F123A
the mutant shows 34% activity compared to the wild type enzyme
F155A
the mutant shows 5% activity compared to the wild type enzyme
H121A
the mutant shows 5% activity compared to the wild type enzyme
H168A
N167A
the mutant shows 121% activity compared to the wild type enzyme
Q119A
the mutant shows 32% activity compared to the wild type enzyme
Q153A
the mutant shows 75% activity compared to the wild type enzyme
Q153E
the mutant shows 60% activity compared to the wild type enzyme
Q153L
the mutant shows 30% activity compared to the wild type enzyme
T245A
the mutant shows 82% activity compared to the wild type enzyme
W179A
the mutant shows less than 2% activity compared to the wild type enzyme
W179N
the mutant shows less than 2% activity compared to the wild type enzyme
Y175F
the mutant shows 62% activity compared to the wild type enzyme
Y214F
the mutant shows less than 2% activity compared to the wild type enzyme
C09S
site-directed mutagenesisthe mutant shows slightly decreased activity compared to the wild-type enzyme
C118S
site-directed mutagenesis, almost inactive mutant
C14S
site-directed mutagenesis, almost inactive mutant
C21S
site-directed mutagenesis, almost inactive mutant
C248S
site-directed mutagenesis, the mutant shows over 95% reduced activity compared to the wild-type enzyme
C27S
site-directed mutagenesis, the mutant shows about 70% reduced activity compared to the wild-type enzyme
C33S
site-directed mutagenesis, the mutant shows about 90% reduced activity compared to the wild-type enzyme
C37S
site-directed mutagenesis, the mutant shows about 50% reduced activity compared to the wild-type enzyme
C46S
site-directed mutagenesis, the mutant shows about 45% reduced activity compared to the wild-type enzyme
C50S
site-directed mutagenesis, the mutant shows 90% reduced activity compared to the wild-type enzyme
C65S
site-directed mutagenesis, the mutant shows 85% reduced activity compared to the wild-type enzyme
C72S
site-directed mutagenesis, the mutant shows over 95% reduced activity compared to the wild-type enzyme
C7S
site-directed mutagenesis, the mutant shows 2fold increased activity compared to the wild-type enzyme
H121A/H124A
-
considerably lower pH dependence for binding than wild-type, cooperativity value around 2 compared to wild-type value of 3.7. Km-value for ascorbate is 3.2 mM compared to 1.9 mM for wild-type enzyme
H121R/H124R
inactive mutant enzyme
H124R
H134A
-
considerably lower pH dependence for binding than wild-type, cooperativity value around 2 compared to wild-type value of 3.7
H167A/H173A
-
considerably lower pH dependence for binding than wild-type, cooperativity value of 1.6 compared to wild-type value of 3.7. Km-value for ascorbate is 8.3 mM compared to 1.9 mM for wild-type enzyme
H167R/H173R
-
considerably lower pH dependence for binding than wild-type, cooperativity value around 2 compared to wild-type value of 3.7. Km-value for ascorbate is 6.3 mM compared to 1.9 mM for wild-type enzyme
V65I
naturally occuring mutation with no change in charge or hydrophobicity
additional information