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Crystal Structure of a Putative Cytochrome P450 Alkane Hydroxylase (CYP153D17) from Sphingomonas sp. PAMC 26605 and Its Conformational Substrate Binding

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Cited 2 time in scopus
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dc.contributor.authorLee, Chang Woo-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorTae-Jin Oh-
dc.contributor.authorPark, Hyun-
dc.contributor.authorPark, Sun-Ha-
dc.contributor.authorJoo-Ho Lee-
dc.contributor.authorSang-Cheol Yu-
dc.date.accessioned2018-03-29T06:14:54Z-
dc.date.available2018-03-29T06:14:54Z-
dc.date.issued2016-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/7505-
dc.description.abstractEnzymatic alkane hydroxylation reactions are useful for producing pharmaceutical and agricultural chemical intermediates from hydrocarbons. Several cytochrome P450 enzymes catalyze the regio- and stereo-specific hydroxylation of alkanes. We evaluated the substrate binding of a putative CYP alkane hydroxylase (CYP153D17) from the bacterium Sphingomonas sp. PAMC 26605. Substrate affinities to C10-C12 n-alkanes and C10-C14 fatty acids with Kd values varied from 0.42 to 0.59 μM. A longer alkane (C12) bound more strongly than a shorter alkane (C10), while shorter fatty acids (C10, capric acid;C12, lauric acid) bound more strongly than a longer fatty acid (C14, myristic acid). These data displayed a broad substrate specificity of CYP153D17 hence it was named as a putative CYP alkane hydroxylase. Moreover, the crystal structure of CYP153D17 was determined at 3.1 A resolution. This is the first study to provide structural information for the CYP153D family. Structural analysis showed that a co-purified alkane-like compound bound near the active-site heme group. The alkane-like substrate is in the hydrophobic pocket containing Thr74, Met90, Ala175, Ile240, Leu241, Val244, Leu292, Met295, and Phe393. Comparison with other CYP structures suggested that conformational changes in the β1-β2, α3-α4, and α6-α7 connecting loop are important for incorporating the long hydrophobic alkane-like substrate. These results improve the understanding of the catalytic mechanism of CYP153D17 and provide valuable information for future protein engineering studies.-
dc.languageEnglish-
dc.titleCrystal Structure of a Putative Cytochrome P450 Alkane Hydroxylase (CYP153D17) from Sphingomonas sp. PAMC 26605 and Its Conformational Substrate Binding-
dc.title.alternative극지 방선균 (Sphingomonas sp. PAMC 26605) 유래 알칸분해효소인 CYP153D17 의 기질결합에 의한 구조변화 연구-
dc.typeArticle-
dc.identifier.bibliographicCitationLee, Chang Woo, et al. 2016. "Crystal Structure of a Putative Cytochrome P450 Alkane Hydroxylase (CYP153D17) from Sphingomonas sp. PAMC 26605 and Its Conformational Substrate Binding". <em>INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES</em>, 17(12): 2067-2067.-
dc.citation.titleINTERNATIONAL JOURNAL OF MOLECULAR SCIENCES-
dc.citation.volume17-
dc.citation.number12-
dc.identifier.doi10.3390/ijms17122067-
dc.citation.startPage2067-
dc.citation.endPage2067-
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2014:46.206-
dc.subject.keywordSphingomonas sp-
dc.subject.keywordX-ray crystallography-
dc.subject.keywordcrystal structure-
dc.subject.keywordcytochrome P450-
dc.subject.keywordsubstrate binding assay-
dc.identifier.localId2016-0257-
dc.identifier.scopusid2-s2.0-85006152292-
dc.identifier.wosid000392280500111-
Appears in Collections  
2014-2016, Antarctic Organisms: Cold-Adaptation Mechanism and Its Application (14-16) / Park; Hyun
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