Identification of an important function of CYP123: Role in the monooxygenase activity in a novel estradiol degradation pathway in bacteria

2021 ◽  
pp. 106025
Author(s):  
Xueying Ye ◽  
Tao Peng ◽  
Yuan Li ◽  
Tongwang Huang ◽  
Hui Wang ◽  
...  
Keyword(s):  
Degradation Pathway ◽  
Monooxygenase Activity

scholarly journals Biotransformation of Indole to 3-Methylindole byLysinibacillus xylanilyticusStrain MA

2015 ◽  
Vol 2015 ◽  
pp. 1-5 ◽  
Author(s):  
Pankaj Kumar Arora ◽  
Kartik Dhar ◽  
Rafael Alejandro Veloz García ◽  
Ashutosh Sharma
Keyword(s):  
Acetic Acid ◽  
Sodium Succinate ◽  
16S Rrna Gene Sequencing ◽  
Transformation Products ◽  
Degradation Pathway ◽  
Gas Chromatography Mass Spectrometry ◽  
Broth Culture ◽  
Rrna Gene ◽  
Monooxygenase Activity ◽  
Indole 3 Acetic Acid

An indole-biotransforming strain MA was identified asLysinibacillus xylanilyticuson the basis of the 16S rRNA gene sequencing. It transforms indole completely from the broth culture in the presence of an additional carbon source (i.e., sodium succinate). Gas-chromatography-mass spectrometry identified indole-3-acetamide, indole-3-acetic acid, and 3-methylindole as transformation products. Tryptophan-2-monooxygenase activity was detected in the crude extracts of indole-induced cells of strain MA, which confirms the formation of indole-3-acetamide from tryptophan in the degradation pathway of indole. On the basis of identified metabolites and enzyme assay, we have proposed a new transformation pathway for indole degradation. Indole was first transformed to indole-3-acetamide via tryptophan. Indole-3-acetamide was then transformed to indole-3-acetic acid that was decarboxylated to 3-methylindole. This is the first report of a 3-methylindole synthesis via the degradation pathway of indole.

scholarly journals Rhodococcus erythropolis DCL14 Contains a Novel Degradation Pathway for Limonene

1999 ◽  
Vol 65 (5) ◽  
pp. 2092-2102 ◽  
Author(s):  
Mariët J. van der Werf ◽  
Henk J. Swarts ◽  
Jan A. M. de Bont
Keyword(s):  
Isocitrate Lyase ◽  
Rhodococcus Erythropolis ◽  
Sole Source ◽  
Degradation Pathway ◽  
Genetic Studies ◽  
Monooxygenase Activity ◽  
Bond Forming ◽  
Activity Product ◽  
Lyase Activity ◽  
Consumption Rates

ABSTRACT Strain DCL14, which is able to grow on limonene as a sole source of carbon and energy, was isolated from a freshwater sediment sample. This organism was identified as a strain of Rhodococcus erythropolis by chemotaxonomic and genetic studies. R. erythropolis DCL14 also assimilated the terpenes limonene-1,2-epoxide, limonene-1,2-diol, carveol, carvone, and (−)-menthol, while perillyl alcohol was not utilized as a carbon and energy source. Induction tests with cells grown on limonene revealed that the oxygen consumption rates with limonene-1,2-epoxide, limonene-1,2-diol, 1-hydroxy-2-oxolimonene, and carveol were high. Limonene-induced cells of R. erythropolis DCL14 contained the following four novel enzymatic activities involved in the limonene degradation pathway of this microorganism: a flavin adenine dinucleotide- and NADH-dependent limonene 1,2-monooxygenase activity, a cofactor-independent limonene-1,2-epoxide hydrolase activity, a dichlorophenolindophenol-dependent limonene-1,2-diol dehydrogenase activity, and an NADPH-dependent 1-hydroxy-2-oxolimonene 1,2-monooxygenase activity. Product accumulation studies showed that (1S,2S,4R)-limonene-1,2-diol, (1S,4R)-1-hydroxy-2-oxolimonene, and (3R)-3-isopropenyl-6-oxoheptanoate were intermediates in the (4R)-limonene degradation pathway. The opposite enantiomers [(1R,2R,4S)-limonene-1,2-diol, (1R,4S)-1-hydroxy-2-oxolimonene, and (3S)-3-isopropenyl-6-oxoheptanoate] were found in the (4S)-limonene degradation pathway, while accumulation of (1R,2S,4S)-limonene-1,2-diol from (4S)-limonene was also observed. These results show thatR. erythropolis DCL14 metabolizes both enantiomers of limonene via a novel degradation pathway that starts with epoxidation at the 1,2 double bond forming limonene-1,2-epoxide. This epoxide is subsequently converted to limonene-1,2-diol, 1-hydroxy-2-oxolimonene, and 7-hydroxy-4-isopropenyl-7-methyl-2-oxo-oxepanone. This lactone spontaneously rearranges to form 3-isopropenyl-6-oxoheptanoate. In the presence of coenzyme A and ATP this acid is converted further, and this finding, together with the high levels of isocitrate lyase activity in extracts of limonene-grown cells, suggests that further degradation takes place via the β-oxidation pathway.

scholarly journals Degradation Pathway of Bisphenol A: Does ipso Substitution Apply to Phenols Containing a Quaternary α-Carbon Structure in the para Position?

2007 ◽  
Vol 73 (15) ◽  
pp. 4776-4784 ◽  
Author(s):  
B. Kolvenbach ◽  
N. Schlaich ◽  
Z. Raoui ◽  
J. Prell ◽  
S. Zühlke ◽  
...  
Keyword(s):  
Bisphenol A ◽  
Degradation Pathway ◽  
Resting Cells ◽  
Enzymatic System ◽  
Type Ii ◽  
Monooxygenase Activity ◽  
Cell Extracts ◽  
Ipso Substitution ◽  
Substitution Mechanism ◽  
Carbon Carbon Bonds

ABSTRACT The degradation of bisphenol A and nonylphenol involves the unusual rearrangement of stable carbon-carbon bonds. Some nonylphenol isomers and bisphenol A possess a quaternary α-carbon atom as a common structural feature. The degradation of nonylphenol in Sphingomonas sp. strain TTNP3 occurs via a type II ipso substitution with the presence of a quaternary α-carbon as a prerequisite. We report here a new degradation pathway of bisphenol A. Consequent to the hydroxylation at position C-4, according to a type II ipso substitution mechanism, the C-C bond between the phenolic moiety and the isopropyl group of bisphenol A is broken. Besides the formation of hydroquinone and 4-(2-hydroxypropan-2-yl)phenol as the main metabolites, further compounds resulting from molecular rearrangements consistent with a carbocationic intermediate were identified. Assays with resting cells or cell extracts of Sphingomonas sp. strain TTNP3 under an 18O2 atmosphere were performed. One atom of 18O2 was present in hydroquinone, resulting from the monooxygenation of bisphenol A and nonylphenol. The monooxygenase activity was dependent on both NADPH and flavin adenine dinucleotide. Various cytochrome P450 inhibitors had identical inhibition effects on the conversion of both xenobiotics. Using a mutant of Sphingomonas sp. strain TTNP3, which is defective for growth on nonylphenol, we demonstrated that the reaction is catalyzed by the same enzymatic system. In conclusion, the degradation of bisphenol A and nonylphenol is initiated by the same monooxygenase, which may also lead to ipso substitution in other xenobiotics containing phenol with a quaternary α-carbon.

Mitochondria Associated Degradation Pathway (MAD) Function Beyond the Outer Membrane

2019 ◽  
Author(s):  
Pin-Chao Liao ◽  
Dana Alessi Wolken ◽  
Edith Serrano ◽  
Pallavi Srivastava ◽  
Liza A. Pon
Keyword(s):  
Outer Membrane ◽  
Degradation Pathway

Corticosteroid Catabolism by Klebsiella pneumoniae as a Possible Mechanism for Increased Pneumonia Risk

2019 ◽  
Vol 20 (4) ◽  
pp. 309-316 ◽  
Author(s):  
Pritam Chattopadhyay ◽  
Goutam Banerjee
Keyword(s):  
Amino Acid ◽  
Klebsiella Pneumoniae ◽  
Kegg Pathway ◽  
Degradation Pathway ◽  
Amino Acid Sequences ◽  
Biological Mechanism ◽  
Clinical Strains ◽  
Catabolism Pathway ◽  
Steroid Catabolism ◽  
Nutrition Source

Background: Several strains of Klebsiella pneumoniae are responsible for causing pneumonia in lung and thereby causing death in immune-suppressed patients. In recent year, few investigations have reported the enhancement of K. pneumoniae population in patients using corticosteroid containing inhaler. Objectives: The biological mechanism(s) behind this increased incidence has not been elucidated. Therefore, the objective of this investigating was to explore the relation between Klebsiella pneumoniae and increment in carbapenamase producing Enterobacteriaceae score (ICS). Methods: The available genomes of K. pneumoniae and the amino acid sequences of steroid catabolism pathway enzymes were taken from NCBI database and KEGG pathway tagged with UniPort database, respectively. We have used different BLAST algorithms (tBLASTn, BLASTp, psiBLAST, and delBLAST) to identify enzymes (by their amino acid sequence) involved in steroid catabolism. Results: A total of 13 enzymes (taken from different bacterial candidates) responsible for corticosteroid degradation have been identified in the genome of K. pneumoniae. Finally, 8 enzymes (K. pneumoniae specific) were detected in four clinical strains of K. pneumoniae. This investigation intimates that this ability to catabolize corticosteroids could potentially be one mechanism behind the increased pneumonia incidence. Conclusion: The presence of corticosteroid catabolism enzymes in K. pneumoniae enhances the ability to utilize corticosteroid for their own nutrition source. This is the first report to demonstrate the corticosteroid degradation pathway in clinical strains of K. pneumoniae.

UV/H2O2 oxidation of tri(2-chloroethyl) phosphate: Intermediate products, degradation pathway and toxicity evaluation

2020 ◽  
Vol 98 ◽  
pp. 55-61 ◽  
Author(s):  
Qiuyi Ji ◽  
Huan He ◽  
Zhanqi Gao ◽  
Xiaohan Wang ◽  
Shaogui Yang ◽  
...  
Keyword(s):  
Degradation Pathway ◽  
Toxicity Evaluation ◽  
Intermediate Products ◽  
H2o2 Oxidation

scholarly journals Further Studies on the 3-Ketosteroid 9α-Hydroxylase of Rhodococcus ruber Chol-4, a Rieske Oxygenase of the Steroid Degradation Pathway

2021 ◽  
Vol 9 (6) ◽  
pp. 1171
Author(s):  
Sara Baldanta ◽  
Juana María Navarro Llorens ◽  
Govinda Guevara
Keyword(s):  
Cholesterol Metabolism ◽  
Genetic Regulation ◽  
Degradation Pathway ◽  
Rhodococcus Ruber ◽  
Promoter Regions ◽  
Steroid Nucleus ◽  
Steroid Substrate ◽  
Fine Regulation ◽  
Rieske Oxygenase ◽  
Steroid Catabolism

The biochemistry and genetics of the bacterial steroid catabolism have been extensively studied during the last years and their findings have been essential to the development of biotechnological applications. For instance, metabolic engineering of the steroid-eater strains has allowed to obtain intermediaries of industrial value. However, there are still some drawbacks that must be overcome, such as the redundancy of the steroid catabolism genes in the genome and a better knowledge of its genetic regulation. KshABs and KstDs are key enzymes involved in the aerobic breakage of the steroid nucleus. Rhodococcus ruber Chol-4 contains three kshAs genes, a single kshB gene and three kstDs genes within its genome. In the present work, the growth of R. ruber ΔkshA strains was evaluated on different steroids substrates; the promoter regions of these genes were analyzed; and their expression was followed by qRT-PCR in both wild type and ksh mutants. Additionally, the transcription level of the kstDs genes was studied in the ksh mutants. The results show that KshA2B and KshA1B are involved in AD metabolism, while KshA3B and KshA1B contribute to the cholesterol metabolism in R. ruber. In the kshA single mutants, expression of the remaining kshA and kstD genes is re-organized to survive on the steroid substrate. These data give insight into the fine regulation of steroid genes when several isoforms are present.

scholarly journals Enhanced Autophagic Activity Improved the Root Growth and Nitrogen Utilization Ability of Apple Plants under Nitrogen Starvation

2021 ◽  
Vol 22 (15) ◽  
pp. 8085
Author(s):  
Liuqing Huo ◽  
Zijian Guo ◽  
Qi Wang ◽  
Li Cheng ◽  
Xin Jia ◽  
...  
Keyword(s):  
Transgenic Plants ◽  
Root Growth ◽  
Nitrogen Starvation ◽  
Degradation Pathway ◽  
Physiological Status ◽  
Hydroponic System ◽  
Nitrogen Levels ◽  
Nitrogen Concentrations ◽  
Nitrogen Nutrients ◽  
Autophagic Activity

Autophagy is a conserved degradation pathway for recycling damaged organelles and aberrant proteins, and its important roles in plant adaptation to nutrient starvation have been generally reported. Previous studies found that overexpression of autophagy-related (ATG) gene MdATG10 enhanced the autophagic activity in apple roots and promoted their salt tolerance. The MdATG10 expression was induced by nitrogen depletion condition in both leaves and roots of apple plants. This study aimed to investigate the differences in the growth and physiological status between wild type and MdATG10-overexpressing apple plants in response to nitrogen starvation. A hydroponic system containing different nitrogen levels was used. The study found that the reduction in growth and nitrogen concentrations in different tissues caused by nitrogen starvation was relieved by MdATG10 overexpression. Further studies demonstrated the increased root growth and the higher nitrogen absorption and assimilation ability of transgenic plants. These characteristics contributed to the increased uptake of limited nitrogen nutrients by transgenic plants, which also reduced the starvation damage to the chloroplasts. Therefore, the MdATG10-overexpressing apple plants could maintain higher photosynthetic ability and possess better growth under nitrogen starvation stress.

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