Transformation of the Recalcitrant Pharmaceutical Compound Carbamazepine byPleurotus ostreatus: Role of Cytochrome P450 Monooxygenase and Manganese Peroxidase

2011 ◽  
Vol 45 (16) ◽  
pp. 6800-6805 ◽  
Author(s):  
Naama Golan-Rozen ◽  
Benny Chefetz ◽  
Julius Ben-Ari ◽  
Joseph Geva ◽  
Yitzhak Hadar
Keyword(s):  
Cytochrome P450 ◽  
Manganese Peroxidase ◽  
Cytochrome P450 Monooxygenase ◽  
P450 Monooxygenase ◽  
Pharmaceutical Compound

scholarly journals Cytochrome P450 Monooxygenase CYP139 Family Involved in the Synthesis of Secondary Metabolites in 824 Mycobacterial Species

2019 ◽  
Vol 20 (11) ◽  
pp. 2690 ◽  
Author(s):  
Puleng Rosinah Syed ◽  
Wanping Chen ◽  
David R. Nelson ◽  
Abidemi Paul Kappo ◽  
Jae-Hyuk Yu ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Amino Acid ◽  
Secondary Metabolites ◽  
Biosynthetic Gene Cluster ◽  
Cytochrome P450 Monooxygenase ◽  
Mycobacterial Species ◽  
P450 Monooxygenase ◽  
Physiological Capacity ◽  
Unique Amino Acid

Tuberculosis (TB) is one of the top infectious diseases causing numerous human deaths in the world. Despite enormous efforts, the physiology of the causative agent, Mycobacterium tuberculosis, is poorly understood. To contribute to better understanding the physiological capacity of these microbes, we have carried out extensive in silico analyses of the 1111 mycobacterial species genomes focusing on revealing the role of the orphan cytochrome P450 monooxygenase (CYP) CYP139 family. We have found that CYP139 members are present in 894 species belonging to three mycobacterial groups: M. tuberculosis complex (850-species), Mycobacterium avium complex (34-species), and non-tuberculosis mycobacteria (10-species), with all CYP139 members belonging to the subfamily “A”. CYP139 members have unique amino acid patterns at the CXG motif. Amino acid conservation analysis placed this family in the 8th among CYP families belonging to different biological domains and kingdoms. Biosynthetic gene cluster analyses have revealed that 92% of CYP139As might be associated with producing different secondary metabolites. Such enhanced secondary metabolic potentials with the involvement of CYP139A members might have provided mycobacterial species with advantageous traits in diverse niches competing with other microbial or viral agents, and might help these microbes infect hosts by interfering with the hosts’ metabolism and immune system.

scholarly journals Interaction of prostacyclin synthase with cytochromes P450

2019 ◽  
Vol 65 (1) ◽  
pp. 63-66
Author(s):  
O.V. Gnedenko ◽  
E.O. Yablokov ◽  
P.V. Ershov ◽  
A.V. Svirid ◽  
T.V. Shkel ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Essential Role ◽  
Protein Complexes ◽  
Cytochromes P450 ◽  
Thromboxane A2 ◽  
Cytochrome P450s ◽  
Cytochrome P450 Monooxygenase ◽  
P450 Monooxygenase ◽  
Prostacyclin Synthase

Biosensor experiments on investigation of interaction between prostacyclin synthase (PGIS) and different proteins of the cytochrome P450 monooxygenase systems were perfomed. Interaction of PGIS with microsomal (CYP21A2, CYP2E1) and mitochondrial (CYP27A1, CYP11B1, CYP11B2, CYP11A1) cytochrome P450s was detected. Kinetic and equilibrium parameters of protein complexes formation were determined. Data obtained suggest an essential role of these hemoproteins interaction in regulation of prostacyclin and thromboxane A2 biosynthesis.

scholarly journals Role of Cytochrome P450 Monooxygenase in the Bioactivation of Aflatoxin B1

2017 ◽  
Vol 46 (9) ◽  
pp. 1499-1503
Author(s):  
Sureeporn Nualkaew ◽  
Hirun Saelim ◽  
Danai Tiwawech ◽  
Tanate Panrat Imran Parvez ◽  
Amornrat Phongdara
Keyword(s):  
Cytochrome P450 ◽  
Aflatoxin B1 ◽  
Cytochrome P450 Monooxygenase ◽  
P450 Monooxygenase

Role of the LolP cytochrome P450 monooxygenase in loline alkaloid biosynthesis

2008 ◽  
Vol 45 (9) ◽  
pp. 1307-1314 ◽  
Author(s):  
Martin J. Spiering ◽  
Jerome R. Faulkner ◽  
Dong-Xiu Zhang ◽  
Caroline Machado ◽  
Robert B. Grossman ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome P450 Monooxygenase ◽  
Alkaloid Biosynthesis ◽  
P450 Monooxygenase

Molecular evolution of a cytochrome P450 for the synthesis of potential antidepressant (2R,6R)-hydroxynorketamine

2021 ◽  
Author(s):  
Ansgar Bokel ◽  
Michael C. Hutter ◽  
Vlada B. Urlacher
Keyword(s):  
Cytochrome P450 ◽  
Molecular Evolution ◽  
Cytochrome P450 Monooxygenase ◽  
P450 Monooxygenase ◽  
Effective Synthesis

Engineered cytochrome P450 monooxygenase CYP154E1 enables the effective synthesis of the potential antidepressant (2R,6R)-hydroxynorketamine via N-demethylation and regio- and stereoselective hydroxylation of (R)-ketamine.

scholarly journals Cytochrome P450 Monooxygenase-Mediated Metabolic Utilization of Benzo[a]Pyrene by Aspergillus Species

mBio ◽  
2019 ◽  
Vol 10 (3) ◽  
Author(s):  
Erin M. Ostrem Loss ◽  
Mi-Kyung Lee ◽  
Ming-Yueh Wu ◽  
Julia Martien ◽  
Wanping Chen ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Environmental Pollutants ◽  
Energy Generation ◽  
Fungal Species ◽  
Metabolic Changes ◽  
Cytochrome P450 Monooxygenase ◽  
Cellular Growth ◽  
P450 Monooxygenase ◽  
Content Type ◽  
Fundamental Knowledge

ABSTRACT Soil-dwelling fungal species possess the versatile metabolic capability to degrade complex organic compounds that are toxic to humans, yet the mechanisms they employ remain largely unknown. Benzo[a]pyrene (BaP) is a pervasive carcinogenic contaminant, posing a significant concern for human health. Here, we report that several Aspergillus species are capable of degrading BaP. Exposing Aspergillus nidulans cells to BaP results in transcriptomic and metabolic changes associated with cellular growth and energy generation, implying that the fungus utilizes BaP as a growth substrate. Importantly, we identify and characterize the conserved bapA gene encoding a cytochrome P450 monooxygenase that is necessary for the metabolic utilization of BaP in Aspergillus. We further demonstrate that the fungal NF-κB-type velvet regulators VeA and VelB are required for proper expression of bapA in response to nutrient limitation and BaP degradation in A. nidulans. Our study illuminates fundamental knowledge of fungal BaP metabolism and provides novel insights into enhancing bioremediation potential. IMPORTANCE We are increasingly exposed to environmental pollutants, including the carcinogen benzo[a]pyrene (BaP), which has prompted extensive research into human metabolism of toxicants. However, little is known about metabolic mechanisms employed by fungi that are able to use some toxic pollutants as the substrates for growth, leaving innocuous by-products. This study systemically demonstrates that a common soil-dwelling fungus is able to use benzo[a]pyrene as food, which results in expression and metabolic changes associated with growth and energy generation. Importantly, this study reveals key components of the metabolic utilization of BaP, notably a cytochrome P450 monooxygenase and the fungal NF-κB-type transcriptional regulators. Our study advances fundamental knowledge of fungal BaP metabolism and provides novel insight into designing and implementing enhanced bioremediation strategies.

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