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1.6.5.4: monodehydroascorbate reductase (NADH)

This is an abbreviated version!
For detailed information about monodehydroascorbate reductase (NADH), go to the full flat file.

Word Map on EC 1.6.5.4

Reaction

NADH
+
H+
+ 2 monodehydroascorbate =
NAD+
+ 2 ascorbate

Synonyms

12-oxophytodienoate reductase 3, AFR reductase, AFR-reductase, AFRR, ascorbate free radical reductase, ascorbate free-radical reductase, ascorbic free radical reductase, At1g63940, At3g09940, AtMDAR1, defensin, MDA, MDA reductase, MDAR, MDAR-OX, MDAR1, MDAR2, MDAR5, MDAsA reductase (NADPH), MDHA, MDHAR, MDHAR1, MDHAR2, MDHAR3, MDHAR6, metallothionein-like type 1 protein, monodehydroascorbate radical reductase, monodehydroascorbate reductase, monodehydroascorbate reductase 2, monodehydroascorbate reductase 4, More, MT-2, MT1K, NADH-semidehydroascorbate oxidoreductase, NADH:AFR oxidoreductase, NADH:ascorbate radical oxidoreductase, NADH:semidehydroascorbic acid oxidoreductase, NEC3, Nectarin III, OPR3, Os09g0567300, peroxisomal monodehydroascorbate reductase, PpMDHAR1, PpMDHAR2, PpMDHAR3, SDA reductase, semidehydroascorbate reductase, Solyc09g009390, SOR, SPD1, thioredoxin H2, Trx h2

ECTree

     1 Oxidoreductases
         1.6 Acting on NADH or NADPH
             1.6.5 With a quinone or similar compound as acceptor
                1.6.5.4 monodehydroascorbate reductase (NADH)

Engineering

Engineering on EC 1.6.5.4 - monodehydroascorbate reductase (NADH)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C70A
about 105% of wild-type activity
E196A
residue E196 forms a hydrogen bond to the O2B molecule in the adenosine ring of NAD. Mutation reduces catalytic activity. Mutant E196A has only about 3 times higher affinity for NAD than that for NADP, i.e. 16fold increase in affinity for NADP compared to the wild-type
G72N
about 70% of wild-type activity
R320A
about 20% of wild-type activity
Y349A
about 10% of wild-type activity
Y349F
about 10% of wild-type activity
Y349W
about 10% of wild-type activity
C69A
mutation has a negligible effect on enzyme activity under standard reaction conditions. The C69A mutant is more resistant to the inhibitory effects of beta-chloromercuribenzoate than the wild type PpMDHAR2 protein
Y345F
mutant is a functional enzyme resistant to inhibition by 0.5 mM and 5.0 mM peroxynitrite
C117A
-
the binding affinity of NADH in the mutant MDAR is lower than that of wild type MDAR as indicated by about 1.5-3fold increase of the Km value for NADH, the mutant is less thermo-stable than the wild type enzyme
C117S
-
the binding affinity of NADH in the mutant MDAR is lower than that of wild type MDAR as indicated by about 1.5-3fold increase of the Km value for NADH, the mutant is less thermo-stable than the wild type enzyme
additional information