Results 1 to 10 of about 55,865 (148)

Xenoestrogen Status of Wuling Farm to Surrounding Water Bodies: An Application of Biochemical Parameters Using Onychostoma barbatulum

open access: yesJournal of Marine Science and Engineering, 2022
The aim of this study was to apply biochemical parameters to Onychostoma barbatulum to understand whether Wuling Farm activities have caused organic pollution from xenoestrogens to flow into surrounding streams and thereby affected area aquatic ...
Lin-Yan Liao   +4 more
doaj   +1 more source

Bioinformatic Mining and Structure-Activity Profiling of Baeyer-Villiger Monooxygenases from Mycobacterium tuberculosis

open access: yesmSphere, 2022
Mycobacterium tuberculosis is the etiological agent of tuberculosis (TB), one of the deadliest infectious diseases. The alarming health context coupled with the emergence of resistant M. tuberculosis strains highlights the urgent need to expand the range
Nicolas Tomas   +15 more
doaj   +1 more source

Carbon and hydrogen stable isotope fractionation due to monooxygenation of short-chain alkanes by butane monooxygenase of Thauera butanivorans Bu-B1211

open access: yesFrontiers in Microbiology, 2023
Multi element compound-specific stable isotope analysis (ME-CSIA) is a tool to assess (bio)chemical reactions of molecules in the environment based on their isotopic fingerprints.
Carsten Vogt   +5 more
doaj   +1 more source

Production of Indigo by Recombinant Escherichia coli with Expression of Monooxygenase, Tryptophanase, and Molecular Chaperone

open access: yesFoods, 2022
Indigo is an important pigment widely used in industries of food, cosmetics, and textile. In this work, the styrene monooxygenase StyAB from Pseudomonas putida was co-expressed with the tryptophanase TnaA and the chaperone groES-groEL in Escherichia coli
Lingyan Du   +3 more
doaj   +1 more source

Alkylglycerol monooxygenase [PDF]

open access: yesIUBMB Life, 2013
AbstractAlkylglycerol monooxygenase (E.C. 1.14.16.5), also called glyceryl ether monooxygenase, is a tetrahydrobiopterin‐dependent enzyme. It is the only enzyme known to cleave the ether bond of alkylglycerols and lyso‐alkylglycerol phospholipids, including lyso‐platelet activating factor.
Watschinger, Katrin, Werner, Ernst R
openaire   +2 more sources

Bacterial flavin-containing monooxygenase is trimethylamine monooxygenase [PDF]

open access: yesProceedings of the National Academy of Sciences, 2011
Flavin-containing monooxygenases (FMOs) are one of the most important monooxygenase systems in Eukaryotes and have many important physiological functions. FMOs have also been found in bacteria; however, their physiological function is not known.
Chen, Yin   +4 more
openaire   +4 more sources

Synthetic Biology Approaches to Hydrocarbon Biosensors: A Review

open access: yesFrontiers in Bioengineering and Biotechnology, 2022
Monooxygenases are a class of enzymes that facilitate the bacterial degradation of alkanes and alkenes. The regulatory components associated with monooxygenases are nature’s own hydrocarbon sensors, and once functionally characterised, these components ...
Claudia F. Moratti   +3 more
doaj   +1 more source

Flavofun: Exploration of fungal flavoproteomes

open access: yesFrontiers in Catalysis, 2022
Fungi produce a plethora of natural products exhibiting a fascinating diversity of chemical structures with an enormous potential for medical applications.
Bianca Kerschbaumer   +2 more
doaj   +1 more source

Identification of an indole biodegradation gene cluster from Providencia rettgeri and its contribution in selectively biosynthesizing Tyrian purple

open access: yesFrontiers in Bioengineering and Biotechnology, 2023
Tyrian purple, mainly composed of 6, 6′-dibromoindigo, is a precious dye extracted from sea snails. In this study, we found Tyrian purple can be selectively produced by a bacterial strain GS-2 when fed with 6-bromotryptophan in the presence of tryptophan.
Feifei Li   +19 more
doaj   +1 more source

Flavoprotein monooxygenases: Versatile biocatalysts

open access: yesBiotechnology Advances, 2021
Flavoprotein monooxygenases (FPMOs) are single- or two-component enzymes that catalyze a diverse set of chemo-, regio- and enantioselective oxyfunctionalization reactions. In this review, we describe how FPMOs have evolved from model enzymes in mechanistic flavoprotein research to biotechnologically relevant catalysts that can be applied for the ...
Paul, Caroline E.   +4 more
openaire   +2 more sources

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