Structural highlights
FunctionPublication Abstract from PubMedAPX is a key antioxidant enzyme in higher plants, scavenging H(2)O(2) with ascorbate in several cellular compartments. Here, we report the crystal structures of cytosolic ascorbate peroxidase from switchgrass (Panicum virgatum L., Pvi), a strategic feedstock plant with several end uses. The overall structure of PviAPX was similar to the structures of other APX family members, with a bound ascorbate molecule at the É£-heme edge pocket as in other APXs. Our results indicated that the H(2)O(2)-dependent oxidation of ascorbate displayed positive cooperativity. Significantly, our study suggested that PviAPX can oxidize a broad range of phenylpropanoids with delta-meso site in a rather similar efficiency, which reflects its role in the fortification of cell walls in response to insect feeding. Based on detailed structural and kinetic analyses and molecular docking, as well as that of closely related APX enzymes, the critical residues in each substrate-binding site of PviAPX are proposed. Taken together, these observations shed new light on the function and catalysis of PviAPX, and potentially benefit efforts improve plant health and biomass quality in bioenergy and forage crops. Activity of Cytosolic Ascorbate Peroxidase (APX) from Panicum virgatum against Ascorbate and Phenylpropanoids.,Zhang B, Lewis JA, Kovacs F, Sattler SE, Sarath G, Kang C Int J Mol Sci. 2023 Jan 16;24(2):1778. doi: 10.3390/ijms24021778. PMID:36675291[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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