Genomic insight into O-demethylation of 4-methoxybenzoate by a two-component system from Amycolatopsis magusensis KCCM40447
Cytochrome P450 monooxygenases perform a multitude of roles, including the generation of hydroxylated aromatic compounds that might be utilized by microorganisms for their survival. WGS data of Amycolatopsis magusensis KCCM40447 revealed a complete circular genome of 9,099,986 base pairs and functio...
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Elsevier
2024-02-01
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author | Bashu Dev Pardhe Lakshan Paudel So-Ra Han Tae-Jin Oh |
author_facet | Bashu Dev Pardhe Lakshan Paudel So-Ra Han Tae-Jin Oh |
author_sort | Bashu Dev Pardhe |
collection | DOAJ |
description | Cytochrome P450 monooxygenases perform a multitude of roles, including the generation of hydroxylated aromatic compounds that might be utilized by microorganisms for their survival. WGS data of Amycolatopsis magusensis KCCM40447 revealed a complete circular genome of 9,099,986 base pairs and functionally assigned 8601 protein-encoding genes. Genomic analysis confirmed that the gene for 4-methoxybenzoate monoxygenase (CYP199A35) was conserved in close proximity to the gene for 4-hydroxybenzoate transporter (PcaK). The co-localized genes encoding CYP199A35, and ferredoxin-NAD(P) reductase (Mbr) represent a two-component system for electron transfer. CYP199A35 was specific for O-demethylation of para O-methyl substituted benzoic acid derivatives, 4-methoxybenzoate (4 MB), and 4-methoxycinnamic acid (4MCA) using the native redox partner (Mbr); two-component system and non-physiological redox partners (Pdr/Pdx); three-component system. The catalytic efficiency for O-demethylation of 4 MB using Mbr and Pdr/Pdx was 0.02 ± 0.006 min−1 μM−1 and 0.07 ± 0.02 min−1 μM−1 respectively. Further, sequence annotation and function prediction by RAST and KEEG analysis revealed a complete catabolic pathway for the utilization of 4 MB by strain KCCM40447, which was also proved experimentally. |
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spelling | doaj.art-631cd3b70e1849e7a0f4f42416ba3a4a2024-02-17T06:39:33ZengElsevierHeliyon2405-84402024-02-01103e25083Genomic insight into O-demethylation of 4-methoxybenzoate by a two-component system from Amycolatopsis magusensis KCCM40447Bashu Dev Pardhe0Lakshan Paudel1So-Ra Han2Tae-Jin Oh3Department of Life Science and Biochemical Engineering, Sun Moon University, Asan, Republic of KoreaDepartment of Life Science and Biochemical Engineering, Sun Moon University, Asan, Republic of KoreaGenome-based BioIT Convergence Institute, Asan, Republic of KoreaDepartment of Life Science and Biochemical Engineering, Sun Moon University, Asan, Republic of Korea; Genome-based BioIT Convergence Institute, Asan, Republic of Korea; Department of Pharmaceutical Engineering and Biotechnology, Sun Moon University, Asan, Republic of Korea; Corresponding author. Department of Life Science and Biochemical Engineering, Sun Moon University, Asan, Republic of Korea.Cytochrome P450 monooxygenases perform a multitude of roles, including the generation of hydroxylated aromatic compounds that might be utilized by microorganisms for their survival. WGS data of Amycolatopsis magusensis KCCM40447 revealed a complete circular genome of 9,099,986 base pairs and functionally assigned 8601 protein-encoding genes. Genomic analysis confirmed that the gene for 4-methoxybenzoate monoxygenase (CYP199A35) was conserved in close proximity to the gene for 4-hydroxybenzoate transporter (PcaK). The co-localized genes encoding CYP199A35, and ferredoxin-NAD(P) reductase (Mbr) represent a two-component system for electron transfer. CYP199A35 was specific for O-demethylation of para O-methyl substituted benzoic acid derivatives, 4-methoxybenzoate (4 MB), and 4-methoxycinnamic acid (4MCA) using the native redox partner (Mbr); two-component system and non-physiological redox partners (Pdr/Pdx); three-component system. The catalytic efficiency for O-demethylation of 4 MB using Mbr and Pdr/Pdx was 0.02 ± 0.006 min−1 μM−1 and 0.07 ± 0.02 min−1 μM−1 respectively. Further, sequence annotation and function prediction by RAST and KEEG analysis revealed a complete catabolic pathway for the utilization of 4 MB by strain KCCM40447, which was also proved experimentally.http://www.sciencedirect.com/science/article/pii/S2405844024011149Cytochrome P450Genomic environmentO-demethylationElectron transfer redox system4-MethoxybenzoateAmycolatopsis magusensis KCCM40447 |
spellingShingle | Bashu Dev Pardhe Lakshan Paudel So-Ra Han Tae-Jin Oh Genomic insight into O-demethylation of 4-methoxybenzoate by a two-component system from Amycolatopsis magusensis KCCM40447 Heliyon Cytochrome P450 Genomic environment O-demethylation Electron transfer redox system 4-Methoxybenzoate Amycolatopsis magusensis KCCM40447 |
title | Genomic insight into O-demethylation of 4-methoxybenzoate by a two-component system from Amycolatopsis magusensis KCCM40447 |
title_full | Genomic insight into O-demethylation of 4-methoxybenzoate by a two-component system from Amycolatopsis magusensis KCCM40447 |
title_fullStr | Genomic insight into O-demethylation of 4-methoxybenzoate by a two-component system from Amycolatopsis magusensis KCCM40447 |
title_full_unstemmed | Genomic insight into O-demethylation of 4-methoxybenzoate by a two-component system from Amycolatopsis magusensis KCCM40447 |
title_short | Genomic insight into O-demethylation of 4-methoxybenzoate by a two-component system from Amycolatopsis magusensis KCCM40447 |
title_sort | genomic insight into o demethylation of 4 methoxybenzoate by a two component system from amycolatopsis magusensis kccm40447 |
topic | Cytochrome P450 Genomic environment O-demethylation Electron transfer redox system 4-Methoxybenzoate Amycolatopsis magusensis KCCM40447 |
url | http://www.sciencedirect.com/science/article/pii/S2405844024011149 |
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