Dehydroascorbate reductase family (DHAR)

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Last update: 2021-12-02 (Bruno Savelli)

Dehydroascorbate reductase family (DHAR)


Glutathione S-transferases (GSTs), previously known as ligandins, comprise a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies: the soluble cytosolic (cGST), mitochondrial (mGST), and membran bound microsomal (MGST). Members of the GST superfamily are extremely diverse in amino acid sequence.
Ascorbate is oxidized by Ascorbate peroxidase (APx) to monodehydroascorbate (MDA), spontanously oxidized into  dehydroascorbate (DHA). MDA and DHA are reduced back to ascorbate by MDA reductase (MDHA) and ferredoxin, and DHA reductase (DHAR).


Dehydroascorbate reductase :
Pfam: PF13417
PF02798 Glutathione S-transferase
N-terminal domain
Interpro: IPR012336
Thioredoxin-like fold; IPR004045
Glutathione S-transferase
N-terminal domain ; IPR010987
Glutathione S-transferase


Tang ZX, Yang HL. Functional divergence and catalytic properties of dehydroascorbate reductase family proteins from Populus tomentosa. Mol Biol Rep. 2013 Aug;40(8):5105-14. PMID:23661023.
Zhang YJ, Wang W, Yang HL, Li Y, Kang XY, Wang XR, Yang ZL. Molecular Properties and Functional Divergence of the Dehydroascorbate Reductase Gene Family in Lower and Higher Plants.PLoS One. 2015 Dec 18;10(12):e0145038. PMID: 26684301.
Shimaoka T, Miyake C, Yokota A. Mechanism of the reaction catalyzed by dehydroascorbate reductase from spinach chloroplasts. Eur J Biochem. 2003 Mar;270(5):921-8. PMID:12603325