CytochromeP450 Enzymes

Abstract

The cytochrome P450 (CYP) enzymes, also known as the microsomal mixed function oxidase system, are the predominant biotransformation pathway in the body for lipid‐soluble endogenous and xenobiotic compounds. CYP enzymes play a key role in the biotransformation of pharmaceutical agents and thus are major determinants of duration of action and clearance of drugs. This article focuses on the characterization, function, and regulation of CYP enzymes that are relevant to our understanding of how CYP enzymes can metabolize a large variety of drugs.

Selective Epoxidation of Fatty Acids and Fatty Acid Methyl Esters by Fungal Peroxygenases

“…The structural determinants driving to selective epoxidations in Mro UPO and Cgl UPO (compared to Aae UPO and Cci UPO) are difficult to be identified with the information available on these new heme‐thiolate enzymes (note that only one UPO crystal structure has been published to date). However, in related P450, epoxidation vs hydroxylation rates have been related to the balance between the iron hydroperoxo and oxenoid forms after the oxidative activation of the enzyme, with an active site threonine being involve in the transition as the proton donor ,. Interestingly, a threonine residue is present at the active sites of both Aae UPO and Cci UPO, and absent from those of Mro UPO and Cgl UPO, as shown by Aranda et al .…”

Thiohydantoins as Potential Antioxidant Agents: In vitro and in silico evaluation

“…CYP enzymes function as part of the NADPH/O 2 − dependent microsomal electron transport system, being the principal ROS source in various tissues and cells. However, the redox reaction can be disturbed, and the uncoupling leads to ROS formation instead of the oxygenated substrate, which lead to DNA damage correlated, for example, with cancer diseases [4–6] …”

Mechanistic studies on versatile metal-assisted hydrogen peroxide activation processes for biomedical and environmental incentives

“…Product analysis experiments provided evidence that both the wild type P450cam enzyme and its mutants are capable of conducting camphor hydroxylation in the presence of hydrogen peroxide. Shunt oxidation reactions with application of H2O2 have also been employed in catalytic oxidation of substrates by other archaeal and bacterial CYPs [95]. For example, the ability to conduct epoxidation of styrene and cis-stilbene by CYP119A1 in the presence of H2O2, has been reported by Koo et al [96] as well as by Rabe et al [97].…”