Results 1 to 10 of about 63,041 (289)

Oxidative modification of free-standing amino acids by Fe(II)/αKG-dependent oxygenases

open access: yesEngineering Microbiology, 2023
Fe(II)/α-ketoglutarate (αKG)-dependent oxygenases catalyze the oxidative modification of various molecules, from DNA, RNA, and proteins to primary and secondary metabolites.
Ikurô Abe, Hui Tao
exaly   +4 more sources

Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases

open access: yesNature Communications, 2020
Rieske oxygenases are iron-dependent enzymes that catalyse C–H mono- and dihydroxylation reactions. Here, the authors characterise two cyanobacterial Rieske oxygenases, SxtT and GxtA that are involved in the biosynthesis of paralytic shellfish toxins and
April L. Lukowski   +3 more
doaj   +2 more sources

Controlled depolymerization of cellulose by light-driven lytic polysaccharide oxygenases

open access: yesNature Communications, 2020
Lytic polysaccharide (mono)oxygenases (LPMOs) perform oxidative cleavage of polysaccharides. Here, the authors showed that the light-driven activity of LPMOs is dependent on hydrogen peroxide availability and can be controlled via the light intensity ...
Bastien Bissaro   +3 more
doaj   +2 more sources

2-Oxoglutarate derivatives can selectively enhance or inhibit the activity of human oxygenases

open access: yesNature Communications, 2021
The human 2-oxoglutarate (2OG) oxygenases FIH and AspH are relevant drug targets. Here, the authors show that synthetic and naturally occurring 2OG derivatives can selectively modulate FIH and AspH activities, suggesting that these compounds may serve as
Yu Nakashima   +4 more
doaj   +2 more sources

The functional differentiation of the post-PKS tailoring oxygenases contributed to the chemical diversities of atypical angucyclines

open access: yesSynthetic and Systems Biotechnology, 2018
Angucyclines are one of the largest families of aromatic polyketides with various chemical structures and bioactivities. Decades of studies have made it easy for us to depict the picture of their early biosynthetic pathways.
Keqiang Fan, Qian Zhang
doaj   +2 more sources

Structure function and engineering of multifunctional non-heme iron dependent oxygenases in fungal meroterpenoid biosynthesis

open access: yesNature Communications, 2018
Non-heme iron and α-ketoglutarate (αKG) oxygenases play a major role in fungal meroterpenoid biosynthesis, but their mechanism remains elusive. Here the authors present crystal structures of two oxygenases, AusE and PrhA, which provide insights into the ...
Yu Nakashima   +7 more
doaj   +2 more sources

Evolutionary aspects and enzymology of metazoan carotenoid cleavage oxygenases

open access: yesBiochimica Et Biophysica Acta - Molecular and Cell Biology of Lipids, 2020
The carotenoids are terpenoid fat-soluble pigments produced by plants, algae, and several bacteria and fungi. They are ubiquitous components of animal diets.
T Michael Redmond   +2 more
exaly   +2 more sources

Industrial Application of 2-Oxoglutarate-Dependent Oxygenases

open access: yesCatalysts, 2019
C–H functionalization is a chemically challenging but highly desirable transformation. 2-oxoglutarate-dependent oxygenases (2OGXs) are remarkably versatile biocatalysts for the activation of C–H bonds. In nature, they have been shown to accept both small
Rebecca Buller, Christin Peters
exaly   +2 more sources

Palmitoylation of Metazoan Carotenoid Oxygenases

open access: yesMolecules, 2020
Abundant in nature, carotenoids are a class of fat-soluble pigments with a polyene tetraterpenoid structure. They possess antioxidant properties and their consumption leads to certain health benefits in humans. Carotenoid cleavage oxygenases (CCOs) are a
T Michael Redmond   +2 more
exaly   +3 more sources

Structural basis of the promiscuity of the unusual Fe(II) and 2-oxoglutarate dependent human aspartate/asparagine-β-hydroxylase [PDF]

open access: yesNature Communications
Protein-hydroxylation catalysed by Fe(II) and 2-oxoglutarate (2OG) dependent oxygenases is an important regulatory mechanism in human biology. Such oxygenases typically coordinate their Fe(II) cofactor via a conserved triad of an aspartate- or glutamate-
Mariska de Munnik   +29 more
doaj   +2 more sources

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