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1.8.5.1: glutathione dehydrogenase (ascorbate)

This is an abbreviated version!
For detailed information about glutathione dehydrogenase (ascorbate), go to the full flat file.

Word Map on EC 1.8.5.1

Reaction

2 glutathione +

dehydroascorbate
=
glutathione disulfide
+
ascorbate

Synonyms

At1g19570, At1g75270, At5g16710, AtDHAR, AtDHAR1, AtDHAR2, AtDHAR3, CrDHAR1, DasA reductase, dehydroascorbate reductase, dehydroascorbate reductase 2, dehydroascorbic acid reductase, dehydroascorbic reductase, dehydrogenase, glutathione (ascorbate), DHA reductase, DHA-R, DHAR, DHAR1, DHAR2, DHAR3, DHAR3a, DHAR4, DHAR5, dioscorin, GDOR, glutathione dehydroascorbate reductase, glutathione-dependent dehydroascorate reductase, glutathione:dehydroascorbic acid oxidoreductase, GRX1, GRX2, GSH-DHAR, GSH:DHA-oxidoreductase, GSTO, GSTO1, GSTO1-1, GSTO2, GSTO2-2, LcDHAR, metallothionein-1, metallothionein-2, More, MT-I, MT-II, nlGSTO, OsDHAR, OsDHAR1, PbDHAR, PgDHAR1, PtrDHAR1, PtrDHAR2, PtrDHAR3A, PtrDHAR3B, SPD1

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.5 With a quinone or similar compound as acceptor
                1.8.5.1 glutathione dehydrogenase (ascorbate)

Engineering

Engineering on EC 1.8.5.1 - glutathione dehydrogenase (ascorbate)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C22A
site-directed mutagenesis, the mutation results in severe loss of the enzyme's function
D21A
site-directed mutagenesis, the mutation results in severe loss of the enzyme's function
D21N
site-directed mutagenesis, the mutation results in severe loss of the enzyme's function
K11A
site-directed mutagenesis, the mutant K11A exhibits about 50% reduced redox activity compared to wild-type
D70A
-
inactive
H95A
-
inactive
H97A
-
the mutant shows wild type activity
Q114H
-
the mutant shows reduced activity compared to the wild type enzyme
A140D
no alteration in specific activity compared to the wild type enzyme
E155
the deletion causes a 2-3fold increase in the specific activity with each substrate and a significant decrease in the enzyme's heat stability, it is also linked to abnormal arsenic excretion patterns
E208K
no alteration in specific activity compared to the wild type enzyme
N142D
no effect on the specific activity of the enzyme with any substrate
Y34A
complete loss of activity
C29A
site-directed mutagenesis, the mutant shows 8.1fold lower activity with dehydroascorbate compared to wild-type
F28A
site-directed mutagenesis, the mutant shows 2.6fold lower activity with dehydroascorbate compared to wild-type
F30L
site-directed mutagenesis, the mutant shows 6.8fold lower activity with dehydroascorbate compared to wild-type
L225A
site-directed mutagenesis, the mutant shows 3.8fold lower activity with dehydroascorbate compared to wild-type
R176A
site-directed mutagenesis, the mutant shows 3.6fold lower activity with dehydroascorbate compared to wild-type
K47A
the mutant shows about wild type activity
K8A
the mutation significantly reduces the enzymatic activity
D72A
reduction in catalytic efficincy. D72 is a glutathione-site residue
K8A
severe reduction in catalytic efficincy. K8 is a glutathione-site residue
S73A
reduction in catalytic efficincy. S73 is a glutathione-site residue
C23S
-
mutant enzyme has almost no activity
C26S
-
turnover number is 57% of the wild-type value, KM-value for dehydroascorbate is 2fold lower than the wild-type value, KM-value for GSH is 1.6old lower than the wild-type value
C9S
-
turnover number is 86% of the wild-type value, KM-value for dehydroascorbate is 2.8fold lower than the wild-type value, KM-value for GSH is 2fold lower than the wild-type value
C9S/C26S
-
turnover number is 43% of the wild-type value, KM-value for dehydroascorbate is 1.1fold higher than the wild-type value, KM-value for GSH is identical to the wild-type value
C25S
-
has equivalent specificity constants for dehydroascorbate and GSH, but may have a different catalytic mechanism
additional information