The peroxidase database
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Classes

Dehydroascorbate reductase family (DHAR)

  Contact author: Christophe Dunand

  Last update: 2018-04-16 (Christophe Dunand)

Dehydroascorbate reductase family (DHAR)

Profiles

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, C-terminal-like

Description

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).

Literature

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

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