Results 81 to 90 of about 33,491 (200)

Tyrosine residues at the substrate binding site in human NQO1 homodimer: Protein conformational dynamics and optimization of substrate binding geometry

open access: yesThe FEBS Journal, EarlyView.
Human NAD(P)H:quinone oxidoreductase 1 is a homodimeric flavoenzyme crucial for redox metabolism and linked to significant health issues. Point mutations at Tyr126 and Tyr128 demonstrate their essential roles in optimizing substrate binding geometry for catalysis, as well as in half‐site reactivity and conformational dynamics during the enzyme's ...
Maribel Rivero   +8 more
wiley   +1 more source

Cryo‐EM structures of multiple‐peptide resistance factor (MprF) from Pseudomonas aeruginosa

open access: yesThe FEBS Journal, EarlyView.
Cryo‐EM analysis of MprF from Pseudomonas aeruginosa reveals a dimeric enzyme, distinct from Rhizobium homologues. The soluble GNAT domain contains a dynamic amphipathic helix (TTH) that adopts different positions in detergent micelle and nanodisc, relative to the membrane.
Shaileshanand Jha, Kutti R. Vinothkumar
wiley   +1 more source

Caffeylpyruvate hydrolase from the bioluminescent fungus Neonothopanus gardneri is the key recycling enzyme in the fungal bioluminescence pathway

open access: yesThe FEBS Journal, EarlyView.
Caffeic acid is a central metabolite in the fungal bioluminescence pathway. We identified and characterized caffeylpyruvate hydrolase from Neonothopanus gardneri (ngarCPH) and demonstrate its ability to hydrolyze fungal oxyluciferin into caffeic and pyruvic acids, confirming a complete and self‐sustained fungal bioluminescence cycle.
Caio K. Zamuner   +8 more
wiley   +1 more source

Aptamer‐mediated outer membrane destabilization overcomes low permeability resistance in Pseudomonas aeruginosa

open access: yesThe FEBS Journal, EarlyView.
DNA aptamers, Apt 60 and Apt 173, target the BamA protein to compromise outer membrane integrity in Pseudomonas aeruginosa, making it susceptible to Azithromycin, an antibiotic that is otherwise poorly effective due to the low‐permeability membrane.
Rupany Selvam   +4 more
wiley   +1 more source

Methods to Study Mitochondrial Metabolism and Homeostasis in Fission Yeast

open access: yes
Yeast, EarlyView.
Ferran Gómez‐Armengol   +2 more
wiley   +1 more source

Cryo‐EM structure of GH43 β‐Xylosidase from Enterobacter cloacae provides insights into substrate specificity and the role of an auxiliary domain in enzymatic activity

open access: yesThe FEBS Journal, EarlyView.
Xylan, the second most abundant plant cell wall polysaccharide, is degraded by β‐xylanases and β‐xylosidases. Here, we present the 2.65 Å cryo‐EM structure of Enterobacter cloacae β‐xylosidase (EcXyl43, GH43) and the 2.4 Å X‐ray structure of its inactive F507A mutant.
Lorenzo Briganti   +8 more
wiley   +1 more source

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