Corrigendum to "Polysaccharide and ethanol extracts of Anoectochilus formosanus Hayata: Antioxidant, wound-healing, antibacterial, and cytotoxic activities".

[This corrects the article DOI: 10.1016/j.heliyon.

Excision of a Protein-Derived Amine for -Aminobenzoate Assembly by the Self-Sacrificial Heterobimetallic Protein CADD.

Chlamydia protein associating with death domains (CADD), the founding member of a recently discovered class of nonheme dimetal enzymes termed hemeoxygenase-like dimetaloxidases (HDOs), plays an indispensable role in pathogen survival. CADD orchestrates the biosynthesis of -aminobenzoic acid (ABA) for integration into folate via the self-sacrificial excision of a protein-derived tyrosine (Tyr27) and several additional processing steps, the nature and timing of which have yet to be fully clarified. Nuclear magnetic resonance (NMR) and proteomics approaches reveal the source and probable timing of amine installation by a neighboring lysine (Lys152).

Polysaccharide and ethanol extracts of Hayata: Antioxidant, wound-healing, antibacterial, and cytotoxic activities.

Introduction: Polysaccharide and alcohol extracts of Hayata have attracted great attention as they exhibit noteworthy properties such as prebiotic and anti-hyperglycemic effects. However, the antioxidant and wound-healing activities of the polysaccharide extract as well as the antibacterial and cytotoxic effects of the ethanol extracts have not been thoroughly uncovered. Therefore, our study investigated these bioactivities of the two extracts prepared from to broaden understandings of medical benefits of the plant.

Distal Hydrophobic Loop Modulates the Copper Active Site and Reaction of AA13 Polysaccharide Monooxygenases.

Polysaccharide monooxygenases (PMOs) use a type-2 copper center to activate O for the selective hydroxylation of one of the two C-H bonds of glycosidic linkages. Our electron paramagnetic resonance (EPR) analysis and molecular dynamics (MD) simulations suggest the unprecedented dynamic roles of the loop containing the residue G89 (G89 loop) on the active site structure and reaction cycle of starch-active PMOs (AA13 PMOs). In the Cu(II) state, the G89 loop could switch between an "open" and "closed" conformation, which is associated with the binding and dissociation of an aqueous ligand in the distal site, respectively.

Self-sacrificial tyrosine cleavage by an Fe:Mn oxygenase for the biosynthesis of -aminobenzoate in .

Chlamydia protein associating with death domains (CADD) is involved in the biosynthesis of -aminobenzoate (pABA), an essential component of the folate cofactor that is required for the survival and proliferation of the human pathogen . The pathway used by for pABA synthesis differs from the canonical multi-enzyme pathway used by most bacteria that relies on chorismate as a metabolic precursor. Rather, recent work showed pABA formation by CADD derives from l-tyrosine.

Fine Tuning of the Copper Active Site in Polysaccharide Monooxygenases.

Type 2 copper active sites, one of the several important copper active sites in biology, were recently found in the novel superfamily of polysaccharide monooxygenases (PMOs) that cleave recalcitrant polysaccharides via an unprecedented oxidative mechanism. The copper center in PMOs is ligated by the bidentate N-terminal histidine residue and another conserved histidine residue, forming a unique T-shaped core termed as . This core serves as the foundation for diverse structures and electronic properties among PMO families and subfamilies.