Same substrate, many reactions: oxygen activation in flavoenzymes
Over time, organisms have evolved strategies to cope with the abundance of dioxygen on
Earth. Oxygen-utilizing enzymes tightly control the reactions involving O2 mostly by …
Earth. Oxygen-utilizing enzymes tightly control the reactions involving O2 mostly by …
Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts
WJH Van Berkel, NM Kamerbeek, MW Fraaije - Journal of biotechnology, 2006 - Elsevier
During the last decades a large number of flavin-dependent monooxygenases have been
isolated and studied. This has revealed that flavoprotein monooxygenases are able to …
isolated and studied. This has revealed that flavoprotein monooxygenases are able to …
[HTML][HTML] Gates of enzymes
Enzymes are very efficient catalysts that are essential for the functioning of living organisms.
The low efficiency of biocatalysts produced de novo relative to those that have evolved …
The low efficiency of biocatalysts produced de novo relative to those that have evolved …
Triepoxide formation by a flavin-dependent monooxygenase in monensin biosynthesis
Q Wang, N Liu, Y Deng, Y Guan, H Xiao… - Nature …, 2023 - nature.com
Monensin A is a prototypical natural polyether polyketide antibiotic. It acts by binding a metal
cation and facilitating its transport across the cell membrane. Biosynthesis of monensin A …
cation and facilitating its transport across the cell membrane. Biosynthesis of monensin A …
Baeyer–Villiger monooxygenases, an emerging family of flavin‐dependent biocatalysts
NM Kamerbeek, DB Janssen… - Advanced Synthesis …, 2003 - Wiley Online Library
Abstract Baeyer–Villiger monooxygenases (BVMOs) are flavoenzymes that catalyze a
remarkably wide variety of oxidative reactions such as regio‐and enantioselective Baeyer …
remarkably wide variety of oxidative reactions such as regio‐and enantioselective Baeyer …
Oxygenases as powerful weapons in the microbial degradation of pesticides
M Cheng, D Chen, RE Parales… - Annual Review of …, 2022 - annualreviews.org
Oxygenases, which catalyze the reductive activation of O2 and incorporation of oxygen
atoms into substrates, are widely distributed in aerobes. They function by switching the …
atoms into substrates, are widely distributed in aerobes. They function by switching the …
Control of catalysis in flavin-dependent monooxygenases
BA Palfey, CA McDonald - Archives of biochemistry and biophysics, 2010 - Elsevier
Flavoprotein monooxygenases reduce flavins, speed their reaction with oxygen, and
stabilize a C4a-oxygen adduct long enough to use this reactive species to transfer an …
stabilize a C4a-oxygen adduct long enough to use this reactive species to transfer an …
Reconstructing NMR spectra of “invisible” excited protein states using HSQC and HMQC experiments
NR Skrynnikov, FW Dahlquist… - Journal of the American …, 2002 - ACS Publications
Carr− Purcell− Meiboom− Gill (CPMG) relaxation measurements employing trains of 180°
pulses with variable pulse spacing provide valuable information about systems undergoing …
pulses with variable pulse spacing provide valuable information about systems undergoing …
Monooxygenation of aromatic compounds by flavin‐dependent monooxygenases
P Chenprakhon, T Wongnate, P Chaiyen - Protein Science, 2019 - Wiley Online Library
Many flavoenzymes catalyze hydroxylation of aromatic compounds especially phenolic
compounds have been isolated and characterized. These enzymes can be classified as …
compounds have been isolated and characterized. These enzymes can be classified as …
Debottlenecking 4-hydroxybenzoate hydroxylation in Pseudomonas putida KT2440 improves muconate productivity from p-coumarate
Abstract The transformation of 4-hydroxybenzoate (4-HBA) to protocatechuate (PCA) is
catalyzed by flavoprotein oxygenases known as para-hydroxybenzoate-3-hydroxylases …
catalyzed by flavoprotein oxygenases known as para-hydroxybenzoate-3-hydroxylases …