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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)

Crystallization

Crystallization on EC 1.6.5.4 - monodehydroascorbate reductase (NADH)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, immediately after purification by hanging drop vapour diffusion method, 0.005 ml of protein solution containing 10 mg/ml protein, mixed with equal volume of reservoir solution containing 20-25% PEG 6000, 0.1 M CaCl2, 50 mM Tris-HCl, pH 8.0, equilibration against 1 ml reservoir solution, 20°C, 1 week, cryoprotection by 30% glycerol, X-ray diffraction structure determination and analysis at 2.4 A resolution
-
3D model of Mdar protein contains 21 sheets and 15 helices and 33 loop regions. The active site is comprised of residues Glu39, Glu40, Glu46, Arg47, Pro48, Lys52, Thr122, Asn147, Tyr173, Pro194, Glu195, Arg201, Ile261, Asn264, Asp299, Glu316, His317, Arg322, Phe347 and Tyr348
structures in the presence of cofactors, NAD+ and NADP+, and complexed with ascorbic acid and isoascorbic acid. The overall structure of MDHAR is similar to other iron-sulfur protein reductases, except for a unique long loop of 63-80 residues, which seems to be essential in forming the active site pocket. Residue Arg320 plays a major substrate binding role, and Tyr349 mediates electron transfer from NAD(P)H to bound substrate via FAD. The enzymatic activity favours NADH as an electron donor over NADPH
to 1.9 A resolution, space group P41212 with unit-cell parameters a, b 81.89 A, c 120.4 A