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H2O2-driven hydroxylation of steroids catalyzed by cytochrome P450 CYP105D18: Exploration of substrate access channel

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dc.contributor.authorBashu Dev Pardhe-
dc.contributor.authorKyoung Pyo Kwon-
dc.contributor.authorJong Kook Park-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorTae-Jin Oh-
dc.date.accessioned2023-02-06T16:37:10Z-
dc.date.available2023-02-06T16:37:10Z-
dc.date.issued2023-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/14321-
dc.description.abstractCYP105D18 supports H2O2 as an oxygen surrogate for catalysis well, and shows high H2O2 resistance capacity. We report the hydroxylation of different steroids using H2O2 as a co-substrate. Testosterone was regiospecifically hydroxylated to 2β-hydroxytestosterone. Based on the experimental data and molecular docking, we predicted that hydroxylation of methyl testosterone and nandrolone would occur at the position 2 in the A-ring, while hydroxylation of androstenedione and adrenosterone was predicted to occur in the B-ring. Further, structure-guided rational design of the substrate access channel was performed with the mutagenesis of residues S63, R82, and F184. Among the mutants, S63A showed a marked decrease in product formation, while F184A showed a significant increase in product formation in testosterone, nandrolone, methyl testosterone, androstenedione, and adrenosterone. The catalytic efficiency (Km/kcat) towards testosterone was increased 1.36-fold in F184A mutant as compared with the wild type enzyme. These findings might facilitate the potential use of CYP105D18 and further engineering to establish the basis of biotechnological applications.-
dc.languageEnglish-
dc.subject.classification해당사항없음-
dc.titleH2O2-driven hydroxylation of steroids catalyzed by cytochrome P450 CYP105D18: Exploration of substrate access channel-
dc.title.alternative토양 미생물 (Streptomyces laurentii) 유래 cytochrome P450 CYP105D18 효소의 스테로이드 기질에 대한 반응 연구-
dc.typeArticle-
dc.identifier.bibliographicCitationBashu Dev Pardhe, et al. 2023. "H2O2-driven hydroxylation of steroids catalyzed by cytochrome P450 CYP105D18: Exploration of substrate access channel". <em>APPLIED AND ENVIRONMENTAL MICROBIOLOGY</em>, 89(1): 1-12.-
dc.citation.titleAPPLIED AND ENVIRONMENTAL MICROBIOLOGY-
dc.citation.volume89-
dc.citation.number1-
dc.identifier.doi10.1128/aem.01585-22-
dc.citation.startPage1-
dc.citation.endPage12-
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2021:28.931-
dc.subject.keywordCytochrome P450-
dc.subject.keywordH2O2-driven hydroxylation-
dc.subject.keywordSite-directed mutagenesis-
dc.subject.keywordSteroid-
dc.identifier.localId2022-0232-
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