{"created":"2025-01-14T00:51:27.678688+00:00","id":2011732,"links":{},"metadata":{"_buckets":{"deposit":"0a4bbd33-edb8-4330-8c9f-484060f87d10"},"_deposit":{"created_by":7,"id":"2011732","owners":[7],"pid":{"revision_id":0,"type":"depid","value":"2011732"},"status":"published"},"_oai":{"id":"oai:tokushima-u.repo.nii.ac.jp:02011732","sets":["1713853213384:1713853295607"]},"author_link":["1262","118","965"],"item_10001_biblio_info_7":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2023-07-29","bibliographicIssueDateType":"Issued"},"bibliographicPageStart":"126070","bibliographicVolumeNumber":"249","bibliographic_titles":[{"bibliographic_title":"International Journal of Biological Macromolecules","bibliographic_titleLang":"en"}]}]},"item_10001_description_5":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"Crystal structures of Pseudomonas veronii L-arginine dehydrogenase (L-ArgDH), belonging to the μ-crystallin/ornithine cyclodeaminase family, were determined for the enzyme in complex with L-lysine and NADP+ and with L-arginine and NADPH. The main chain coordinates of the P. veronii L-ArgDH monomer showed notable similarity to those of Archaeoglobus fulgidus L-AlaDH, belonging to the same family, and pro-R specificity similar to L-AlaDH for hydride transfer to NADP+ was postulated. However, the residues recognizing the α-amino group of the substrates differed between the two enzymes. Based on a substrate modeling study, it was proposed that in A. fulgidus L-AlaDH, the amino group of L-alanine interacts via a water molecule (W510) with the side chains of Lys41 and Arg52. By contrast, the α-amino group of L-arginine formed hydrogen bonds with the side chains of Thr224 and Asn225 in P. veronii L-ArgDH. Moreover, the guanidino group of L-arginine was fixed into the active site via hydrogen bonds with the side chain of Asp54. Site-directed mutagenesis suggested that Asp54 plays an important role in maintaining high reactivity against the substrate and that Tyr58 and Lys71 play critical roles in enzyme catalysis.","subitem_description_language":"en","subitem_description_type":"Abstract"}]},"item_10001_publisher_8":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"Elsevier","subitem_publisher_language":"en"}]},"item_10001_rights_15":{"attribute_name":"権利情報","attribute_value_mlt":[{"subitem_rights":"© 2023. This manuscript version is made available under the CC-BY-NC-ND 4.0 license https://creativecommons.org/licenses/by-nc-nd/4.0/","subitem_rights_language":"en"}]},"item_10001_source_id_9":{"attribute_name":"収録物ID","attribute_value_mlt":[{"subitem_source_identifier":"01418130","subitem_source_identifier_type":"ISSN"},{"subitem_source_identifier":"18790003","subitem_source_identifier_type":"ISSN"},{"subitem_source_identifier":"AA00233999","subitem_source_identifier_type":"NCID"},{"subitem_source_identifier":"AA1153092X","subitem_source_identifier_type":"NCID"}]},"item_10001_version_type_20":{"attribute_name":"出版タイプ","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_ab4af688f83e57aa","subitem_version_type":"AM"}]},"item_1715043197608":{"attribute_name":"アクセス権","attribute_value_mlt":[{"subitem_access_right":"open 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