7f8s
From Proteopedia
Jump to navigationJump to search
Pennisetum glaucum (Pearl millet) dehydroascorbate reductase (DHAR) with catalytic cysteine (Cy20) in sulphenic and sulfinic acid forms.
| ||||||||||||
Structural highlights
FunctionPublication Abstract from PubMedAscorbate is an important cellular antioxidant that gets readily oxidized to dehydroascorbate (DHA). Recycling of DHA is therefore paramount in the maintenance of cellular homeostasis and preventing oxidative stress. Dehydroascorbate reductases (DHARs), in conjunction with glutathione (GSH), carry out this vital process in eukaryotes, among which plant DHARs have garnered considerable attention. A detailed kinetic analysis of plant DHARs relative to their human counterparts is, however, lacking. Chloride intracellular channels (HsCLICs) are close homologs of plant DHARs, recently demonstrated to share their enzymatic activity. This study reports the highest turnover rate for a plant DHAR from stress adapted Pennisetum glaucum (PgDHAR). In comparison, HsCLICs 1, 3, and 4 reduced DHA at a significantly lower rate. We further show that the catalytic cysteine from both homologs was susceptible to varying degrees of oxidation, validated by crystal structures and mass-spectrometry. Our findings may have broader implications on crop improvement using pearl millet DHAR vis-a-vis discovery of cancer therapeutics targeting Vitamin-C recycling capability of human CLICs. Comparative kinetic analysis of ascorbate (Vitamin-C) recycling dehydroascorbate reductases from plants and humans.,Das BK, Kumar A, Sreekumar SN, Ponraj K, Gadave K, Kumar S, Murali Achary VM, Ray P, Reddy MK, Arockiasamy A Biochem Biophys Res Commun. 2021 Dec 29;591:110-117. doi:, 10.1016/j.bbrc.2021.12.103. PMID:35007834[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
This page was last modified 17:11, 29 November 2023.