scholarly journals Mutagenesis of certain activated carcinogens in vitro associated with genetically mediated increases in monooxygenase activity and cytochrome P 1-450.

1975 ◽  
Vol 250 (17) ◽  
pp. 6769-6778
Author(s):  
J S Felton ◽  
D W Nebert
Keyword(s):  
Monooxygenase Activity

Flavin-Containing Monooxygenase Activity in Hepatocytes and Microsomes: In Vitro Characterization and In Vivo Scaling of Benzydamine Clearance

2002 ◽  
Vol 30 (10) ◽  
pp. 1087-1093 ◽  
Author(s):  
Michael B. Fisher ◽  
Kwansik Yoon ◽  
Marcie L. Vaughn ◽  
Timothy J. Strelevitz ◽  
Robert S. Foti
Keyword(s):  
Monooxygenase Activity ◽  
In Vitro Characterization

scholarly journals Characterised Flavin-Dependent Two-Component Monooxygenases from the CAM Plasmid of Pseudomonas putida ATCC 17453 (NCIMB 10007): ketolactonases by Another Name

2018 ◽  
Vol 7 (1) ◽  
pp. 1 ◽  
Author(s):  
Andrew Willetts
Keyword(s):  
Pseudomonas Putida ◽  
Mode Of Action ◽  
Enzyme System ◽  
Monooxygenase Activity ◽  
Two Component ◽  
Functional Understanding ◽  
Dependent Growth

The CAM plasmid-coded isoenzymic diketocamphane monooxygenases induced in Pseudomonas putida ATCC 17453 (NCIMB 10007) by growth of the bacterium on the bicyclic monoterpene (rac)-camphor are notable both for their interesting history, and their strategic importance in chemoenzymatic syntheses. Originally named ‘ketolactonase—an enzyme system for cyclic lactonization’ because of its characterised mode of action, (+)-camphor-induced 2,5-diketocamphane 1,2-monooxygenase was the first example of a Baeyer-Villiger monooxygenase activity to be confirmed in vitro. Both this enzyme and the enantiocomplementary (−)-camphor-induced 3,6-diketocamphane 1,6-monooxygenase were mistakenly classified and studied as coenzyme-containing flavoproteins for nearly 40 years before being correctly recognised and reinvestigated as FMN-dependent two-component monooxygenases. As has subsequently become evident, both the nature and number of flavin reductases able to supply the requisite reduced flavin co-substrate for the monooxygenases changes progressively throughout the different phases of camphor-dependent growth. Highly purified preparations of the enantiocomplementary monooxygenases have been exploited successfully for undertaking both nucleophilic and electrophilic biooxidations generating various enantiopure lactones and sulfoxides of value as chiral synthons and auxiliaries, respectively. In this review the chequered history, current functional understanding, and scope and value as biocatalysts of the diketocamphane monooxygenases are discussed.

scholarly journals In Vitro Metabolic Fate of the Synthetic Cannabinoid Receptor Agonists QMPSB and QMPCB (SGT-11) Including Isozyme Mapping and Esterase Activity

Metabolites ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 509
Author(s):  
Matthias J. Richter ◽  
Lea Wagmann ◽  
Tanja M. Gampfer ◽  
Simon D. Brandt ◽  
Markus R. Meyer
Keyword(s):  
Human Liver ◽  
Cannabinoid Receptor ◽  
Ester Hydrolysis ◽  
Synthetic Cannabinoid ◽  
Toxicological Screening ◽  
Metabolic Fate ◽  
Monooxygenase Activity ◽  
Receptor Agonists ◽  
Synthetic Cannabinoid Receptor Agonists

Quinolin-8-yl 4-methyl-3-(piperidine-1-sulfonyl)benzoate (QMPSB) and quinolin-8-yl 4-methyl-3-(piperidine-1-carbonyl)benzoate (QMPCB, SGT-11) are synthetic cannabinoid receptor agonists (SCRAs). Knowing their metabolic fate is crucial for the identification of toxicological screening targets and to predict possible drug interactions. The presented study aimed to identify the in vitro phase I/II metabolites of QMPSB and QMPCB and to study the contribution of different monooxygenases and human carboxylesterases by using pooled human liver S9 fraction (pHLS9), recombinant human monooxygenases, three recombinant human carboxylesterases, and pooled human liver microsomes. Analyses were carried out by liquid chromatography high-resolution tandem mass spectrometry. QMPSB and QMPCB showed ester hydrolysis, and hydroxy and carboxylic acid products were detected in both cases. Mono/dihydroxy metabolites were formed, as were corresponding glucuronides and sulfates. Most of the metabolites could be detected in positive ionization mode with the exception of some QMPSB metabolites, which could only be found in negative mode. Monooxygenase activity screening revealed that CYP2B6/CYP2C8/CYP2C9/CYP2C19/CYP3A4/CYP3A5 were involved in hydroxylations. Esterase screening showed the involvement of all investigated isoforms. Additionally, extensive non-enzymatic ester hydrolysis was observed. Considering the results of the in vitro experiments, inclusion of the ester hydrolysis products and their glucuronides and monohydroxy metabolites into toxicological screening procedures is recommended.

Reconstitution of monooxygenase activity of membrane cytochromes P450 in vitro and detergents

2007 ◽  
Vol 415 (1) ◽  
pp. 174-178 ◽  
Author(s):  
K. N. Myasoedova ◽  
A. M. Arutyunyan ◽  
N. N. Magretova
Keyword(s):  
Cytochromes P450 ◽  
Monooxygenase Activity
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