Structural highlights
Function
[APR1_ARATH] Reduces sulfate for Cys biosynthesis. Substrate preference is adenosine-5'-phosphosulfate (APS) >> 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Uses glutathione or DTT as source of protons.
Publication Abstract from PubMed
Sulfur is an essential nutrient that can be converted into utilizable metabolic forms to produce sulfur-containing metabolites in plant. Adenosine 5'-phosphosulfate (APS) reductase (APR) plays a vital role in catalyzing the reduction of activated sulfate to sulfite, which requires glutathione. Previous studies have shown that the C-terminal domain of APR acts as a glutathione-dependent reductase. The crystal structure of the C-terminal redox domain of Arabidopsis APR1 (AtAPR1) shows a conserved alpha/beta thioredoxin fold, but not a glutaredoxin fold. Further biochemical studies of the redox domain from AtAPR1 provided evidence to support the structural observation. Collectively, our results provide structural and biochemical information to explain how the thioredoxin fold exerts the glutaredoxin function in APR.
C-terminal Redox Domain of Arabidopsis APR1 is a Non-Canonical Thioredoxin Domain with Glutaredoxin Function.,Chen FF, Chien CY, Cho CC, Chang YY, Hsu CH Antioxidants (Basel). 2019 Oct 8;8(10). pii: antiox8100461. doi:, 10.3390/antiox8100461. PMID:31597378[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen FF, Chien CY, Cho CC, Chang YY, Hsu CH. C-terminal Redox Domain of Arabidopsis APR1 is a Non-Canonical Thioredoxin Domain with Glutaredoxin Function. Antioxidants (Basel). 2019 Oct 8;8(10). pii: antiox8100461. doi:, 10.3390/antiox8100461. PMID:31597378 doi:http://dx.doi.org/10.3390/antiox8100461
