{"created":"2023-06-19T07:26:02.693327+00:00","id":14277,"links":{},"metadata":{"_buckets":{"deposit":"4356bd0d-ca61-46aa-a58e-a3d92e85fb95"},"_deposit":{"created_by":118,"id":"14277","owners":[118],"pid":{"revision_id":0,"type":"depid","value":"14277"},"status":"published"},"_oai":{"id":"oai:gifu-pu.repo.nii.ac.jp:00014277","sets":["212:276:279"]},"author_link":["33000","32999","33001","32997","32998","33002"],"item_3_biblio_info_3":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2020-06-04","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"3","bibliographicPageEnd":"732","bibliographicPageStart":"728","bibliographicVolumeNumber":"526","bibliographic_titles":[{},{"bibliographic_title":"Biochemical and Biophysical Research Communications","bibliographic_titleLang":"en"}]}]},"item_3_text_4":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_text_value":" 10.1016/j.bbrc.2020.03.176 "}]},"item_3_textarea_2":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_textarea_value":"1,5-Anhydro-D-fructose (AF), a metabolite of the anhydrofructose pathway of glycogen metabolism, has recently been shown to react with intracellular proteins and form advanced glycation end-products. The reactive AF is metabolized to non-reactive 1,5-anhydro-D-glucitol by AF reductase in animal tissues and human cells. Pig and mouse AF reductases were characterized, but primate AF reductase remains unknown. Here, we examined the AF-reducing activity of eleven primate NADPH-dependent reductases with broad substrate specificity for carbonyl compounds. AF was reduced by monkey dimeric dihydrodiol dehydrogenase (DHDH), human aldehyde reductase (AKR1A1) and human dicarbonyl/L-xylulose reductase (DCXR). DHDH showed the lowest KM (21 μM) for AF, and its kcat/KM value (1208 s-1mM-1) was much higher than those of AKR1A1 (1.3 s-1mM-1), DCXR (1.1 s-1mM-1) and the pig and mouse AF reductases. AF is a novel substrate with higher affinity and catalytic efficiency than known substrates of DHDH. Docking simulation study suggested that Lys156 in the substrate-binding site of DHDH contributes to the high affinity for AF. Gene database searches identified DHDH homologues (with >95% amino acid sequence identity) in humans and apes. Thus, DHDH acts as an efficient AF reductase in primates. "}]},"item_access_right":{"attribute_name":"アクセス権","attribute_value_mlt":[{"subitem_access_right":"metadata only access","subitem_access_right_uri":"http://purl.org/coar/access_right/c_14cb"}]},"item_keyword":{"attribute_name":"キーワード","attribute_value_mlt":[{"subitem_subject":"1,5-Anhydro-D-fructose reductase; 1,5-Anhydro-D-glucitol; AKR1A1; D-xylose dehydrogenase; DHDH; Dicarbonyl/L-xylulose reductase.","subitem_subject_language":"en","subitem_subject_scheme":"Other"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"eng"}]},"item_resource_type":{"attribute_name":"資源タイプ","attribute_value_mlt":[{"resourcetype":"journal article","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"Dimeric dihydrodiol dehydrogenase is an efficient primate 1,5-anhydro-D-fructose reductase","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Dimeric dihydrodiol dehydrogenase is an efficient primate 1,5-anhydro-D-fructose reductase","subitem_title_language":"en"}]},"item_type_id":"3","owner":"118","path":["279"],"pubdate":{"attribute_name":"公開日","attribute_value":"2021-03-04"},"publish_date":"2021-03-04","publish_status":"0","recid":"14277","relation_version_is_last":true,"title":["Dimeric dihydrodiol dehydrogenase is an efficient primate 1,5-anhydro-D-fructose reductase"],"weko_creator_id":"118","weko_shared_id":-1},"updated":"2023-06-19T07:44:28.977504+00:00"}