Monodehydroascorbate reductase (NADH)

Monodehydroascorbate reductase (NADH)
monodehydroascorbate reductase (NADH)
Identifiers
EC number 1.6.5.4
CAS number 9029-26-9
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, a monodehydroascorbate reductase (NADH) (EC 1.6.5.4) is an enzyme that catalyzes the chemical reaction

NADH + H+ + 2 monodehydroascorbate \rightleftharpoons NAD+ + 2 ascorbate

The 3 substrates of this enzyme are NADH, H+, and monodehydroascorbate, whereas its two products are NAD+ and ascorbate.

This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a quinone or similar compound as acceptor. The systematic name of this enzyme class is NADH:monodehydroascorbate oxidoreductase. Other names in common use include NADH:semidehydroascorbic acid oxidoreductase, MDHA, semidehydroascorbate reductase, AFR, AFR-reductase, ascorbic free radical reductase, ascorbate free radical reductase, SOR, MDAsA reductase (NADPH), SDA reductase, NADH:ascorbate radical oxidoreductase, NADH-semidehydroascorbate oxidoreductase, ascorbate free-radical reductase, NADH:AFR oxidoreductase, and monodehydroascorbate reductase (NADH2). This enzyme participates in ascorbate and aldarate metabolism.

In plants, the monodehydroascorbate reductase (MDAR) is an enzymatic component of the glutathione-ascorbate cycle that is one of the major antioxidant systems of plant cells for the protection against the damages produced by reactive oxygen species (ROS). The MDAR activity has been described in several cell compartments, such as chloroplasts, cytosol, mitochondria, glyoxysomes, and leaf peroxisomes. [1].

References

  1. ^ Leterrier M et al. (2005). "Peroxisomal monodehydroascorbate reductase. Genomic clone characterization and functional analysis under environmental stress conditions.". Plant Physiol 138 (4): 2111–23.. doi:10.1104/pp.105.066225. PMC 1183399. PMID 16055677. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1183399. 
  • Schulze HU, Schott HH, Staudinger H (1972). "[The isolation and characterization of a NADH: semidehydroascorbic acid oxidoreductase from Neurospora crassa]". Hoppe. Seylers. Z. Physiol. Chem. 353 (12): 1931–42. PMID 4405497. 
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