Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex
DC Field | Value | Language |
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dc.contributor.author | Kim, Jun Hoe | - |
dc.contributor.author | Kim, Bong Heon | - |
dc.contributor.author | Brooks, Shelby | - |
dc.contributor.author | Kang, Seung Yeon | - |
dc.contributor.author | Summers, Ryan M. | - |
dc.contributor.author | Song, Hyun Kyu | - |
dc.date.accessioned | 2021-09-01T07:11:09Z | - |
dc.date.available | 2021-09-01T07:11:09Z | - |
dc.date.created | 2021-06-19 | - |
dc.date.issued | 2019-09-06 | - |
dc.identifier.issn | 0022-2836 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/62898 | - |
dc.description.abstract | Caffeine, found in many foods, beverages, and pharmaceuticals, is the most used chemical compound for mental alertness. It is originally a natural product of plants and exists widely in environmental soil. Some bacteria, such as Pseudomonas putida CBB5, utilize caffeine as a sole carbon and nitrogen source by degrading it through sequential N-demethylation catalyzed by five enzymes (NdmA, NdmB, NdmC, NdmD, and NdmE). The environmentally friendly enzymatic reaction products, methylxanthines, are high-value biochemicals that are used in the pharmaceutical and cosmetic industries. However, the structures and biochemical properties of bacterial N-demethylases remain largely unknown. Here, we report the structures of NdmA and NdmB, the initial N-1- and N-3-specific demethylases, respectively. Reverse-oriented substrate bindings were observed in the substrate-complexed structures, offering methyl position specificity for proper N-demethylation. For efficient sequential degradation of caffeine, these enzymes form a unique heterocomplex with 3:3 stoichiometry, which was confirmed by enzymatic assays, fluorescent labeling, and small-angle x-ray scattering. The binary structure of NdmA with the ferredoxin domain of NdmD, which is the first structural information for the plant-type ferredoxin domain in a complex state, was also determined to better understand electron transport during N-demethylation. These findings broaden our understanding of the caffeine degradation mechanism by bacterial enzymes and will enable their use for industrial applications. (C) 2019 Elsevier Ltd. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | - |
dc.subject | POLYCYCLIC AROMATIC-HYDROCARBONS | - |
dc.subject | NAPHTHALENE DIOXYGENASE | - |
dc.subject | CRYSTAL-STRUCTURE | - |
dc.subject | DICAMBA MONOOXYGENASE | - |
dc.subject | STRUCTURE REFINEMENT | - |
dc.subject | OXYGENASE COMPONENT | - |
dc.subject | ACTIVE-SITE | - |
dc.subject | NONHEME | - |
dc.subject | SPECIFICITY | - |
dc.subject | SYSTEM | - |
dc.title | Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Song, Hyun Kyu | - |
dc.identifier.doi | 10.1016/j.jmb.2019.08.004 | - |
dc.identifier.scopusid | 2-s2.0-85071119666 | - |
dc.identifier.wosid | 000487168300004 | - |
dc.identifier.bibliographicCitation | JOURNAL OF MOLECULAR BIOLOGY, v.431, no.19, pp.3647 - 3661 | - |
dc.relation.isPartOf | JOURNAL OF MOLECULAR BIOLOGY | - |
dc.citation.title | JOURNAL OF MOLECULAR BIOLOGY | - |
dc.citation.volume | 431 | - |
dc.citation.number | 19 | - |
dc.citation.startPage | 3647 | - |
dc.citation.endPage | 3661 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.subject.keywordPlus | POLYCYCLIC AROMATIC-HYDROCARBONS | - |
dc.subject.keywordPlus | NAPHTHALENE DIOXYGENASE | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | DICAMBA MONOOXYGENASE | - |
dc.subject.keywordPlus | STRUCTURE REFINEMENT | - |
dc.subject.keywordPlus | OXYGENASE COMPONENT | - |
dc.subject.keywordPlus | ACTIVE-SITE | - |
dc.subject.keywordPlus | NONHEME | - |
dc.subject.keywordPlus | SPECIFICITY | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.subject.keywordAuthor | caffeine | - |
dc.subject.keywordAuthor | N-demethylase | - |
dc.subject.keywordAuthor | plant-type ferredoxin | - |
dc.subject.keywordAuthor | rational protein engineering | - |
dc.subject.keywordAuthor | reductase | - |
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