2020
DOI: 10.1186/s40643-019-0290-4
|View full text |Cite
|
Sign up to set email alerts
|

Bacterial cytochrome P450-catalyzed regio- and stereoselective steroid hydroxylation enabled by directed evolution and rational design

Abstract: Steroids are the most widely marketed products by the pharmaceutical industry after antibiotics. Steroid hydroxylation is one of the most important functionalizations because their derivatives enable a higher biological activity compared to their less polar non-hydroxylated analogs. Bacterial cytochrome P450s constitute promising biocatalysts for steroid hydroxylation due to their high expression level in common workhorses like Escherichia coli. However, they often suffer from wrong or insufficient regio-and/o… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

0
45
0

Year Published

2020
2020
2022
2022

Publication Types

Select...
10

Relationship

3
7

Authors

Journals

citations
Cited by 64 publications
(45 citation statements)
references
References 101 publications
0
45
0
Order By: Relevance
“…Cytochrome P450 (CYP) enzymes are heme monooxygenases [ 194 ] and named after the absorption band at 450 nm observed after binding of carbon monoxide [ 195 , 196 , 197 ]. They are found across all members of the three life domains, bacteria, archea and eukarya [ 198 , 199 , 200 , 201 , 202 ] and have crucial roles in detoxification of drugs and xenobiotics but also in the anabolism of sterols, fatty acids, eicosanoids, and vitamins [ 203 , 204 ]. CYP enzymes have also been shown to generate, similar to COX and LOX enzymes, prostaglandins and leukotrienes from AA as substrate as well as products from concerted reactions with LOX, like hydroxyeicosatetraenoic acids [ 205 , 206 ].…”
Section: Cellular Ros Sourcesmentioning
confidence: 99%
“…Cytochrome P450 (CYP) enzymes are heme monooxygenases [ 194 ] and named after the absorption band at 450 nm observed after binding of carbon monoxide [ 195 , 196 , 197 ]. They are found across all members of the three life domains, bacteria, archea and eukarya [ 198 , 199 , 200 , 201 , 202 ] and have crucial roles in detoxification of drugs and xenobiotics but also in the anabolism of sterols, fatty acids, eicosanoids, and vitamins [ 203 , 204 ]. CYP enzymes have also been shown to generate, similar to COX and LOX enzymes, prostaglandins and leukotrienes from AA as substrate as well as products from concerted reactions with LOX, like hydroxyeicosatetraenoic acids [ 205 , 206 ].…”
Section: Cellular Ros Sourcesmentioning
confidence: 99%
“…Cytochrome P450 catalyses the oxidation of a variety of substrates within the body such as N -palmitoylglycine (NPG) (Zhang et al, 2020 ). Within the enzyme, the BM3Heme domain is responsible for substrate binding but requires the partner redox domain in order to be catalytically competent.…”
Section: Resultsmentioning
confidence: 99%
“…When entering the cells of pro- and eukaryotes, saccharin may be affected by high pH values and by a whole complex of enzymes, including the cytochrome P450 superfamily (CYPs; EC 1.14.14.1), which catalyzes the oxidation of the compounds with aliphatic or aromatic rings [ 45 , 46 , 47 , 48 , 49 , 50 , 51 , 52 , 53 ]. Given this, it is obvious that the isothiazolidinic ring of o -benzoic sulfimide can undergo chemical and/or enzymatic decyclization.…”
Section: Mechanism Of the Biogenic Transformation Of Saccharinmentioning
confidence: 99%