{"id":449,"date":"2024-01-16T16:25:58","date_gmt":"2024-01-16T15:25:58","guid":{"rendered":"https:\/\/asa-enzyme.de\/?post_type=product&#038;p=449"},"modified":"2026-03-02T15:33:33","modified_gmt":"2026-03-02T14:33:33","slug":"l-leucine-dehydrogenase","status":"publish","type":"product","link":"https:\/\/asa-enzyme.de\/de\/produkt\/l-leucine-dehydrogenase\/","title":{"rendered":"L-leucine-dehydrogenase"},"content":{"rendered":"<div class=\"page-header\">\n<h2>L-leucine dehydrogenase<\/h2>\n<\/div>\n<div>\n<h6><span lang=\"en\">EC 1.4.1.9<\/span><\/h6>\n<h6><span lang=\"en\">Oxidoreductase<\/span><\/h6>\n<h6><span lang=\"en\"><strong>Aus<\/strong>\u00a0<em>Bacillus cereus<\/em><\/span><\/h6>\n<p><span lang=\"en\"><strong>Anwendung:<\/strong> L-leucine-dehydrogenase katalysiert die oxidative Desaminierung von L-Leucin, L-Valin und L-Isoleucin sowie von Aminos\u00e4uren mit unverzweigter aliphatischer Carbons\u00e4urekette.\nDurch die R\u00fcckreaktion werden zahlreiche 2-Ketos\u00e4uren, insbesondere 2-Isocapronat, 2-Ketoisovalerat und 2-Keto-3-methylvalerat, mit 0,9 M Am-monium reduktiv zur entsprechenden Aminos\u00e4ure aminiert.<\/span><span id=\"result_box\" lang=\"en\">.<\/span><\/p>\n<p><span lang=\"en\"><strong>Aktivit\u00e4t:<\/strong> &gt; 50 U\/mL<\/span><\/p>\n<p><span lang=\"en\"><strong>Artikel Nr.:<\/strong>\u00a01410<\/span><\/p>\n<p><strong><span lang=\"en\">Produktdatenblatt DE <a href=\"https:\/\/asa-enzyme.de\/wp-content\/uploads\/2025\/09\/PDB-L-Leucine-dehydrogenase-1410-DE.pdf\" target=\"_blank\" rel=\"noopener\">LeucinDH &#8211; 1410 &#8211; DE<\/a><\/span><\/strong><\/p>\n<p><strong>Produktdatenblatt ENG <a href=\"https:\/\/asa-enzyme.de\/wp-content\/uploads\/2025\/09\/PDS-L-Leucine-dehydrogenase-1410-ENG.pdf\" target=\"_blank\" rel=\"noopener\"><span lang=\"en\">LeucinDH &#8211; 1410 &#8211; ENG<\/span><\/a><\/strong><\/p>\n<p><strong>Sicherheitsdatenblatt:\u00a0<\/strong>Auf Anfrage<\/p>\n<p><strong>Wissenschaftliche Literatur\u00a0<\/strong><\/p>\n<p id=\"screen-reader-main-title\" class=\"Head u-font-serif u-h2 u-margin-s-ver\"><span class=\"title-text\"><a href=\"https:\/\/www.sciencedirect.com\/science\/article\/abs\/pii\/000398616290245X?via%3Dihub\" target=\"_blank\" rel=\"noopener\">The distribution and substrate specificity of <span class=\"small-caps\">l<\/span>-leucine dehydrogenase<\/a> (By M.W. Zink, B.D. Sanwal; 1962;\u00a0<em>Archives of Biochemistry and Biophysics,\u00a0<\/em>Volume 99, Issue 1, October 1962, Pages 72-77; DOI: <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/abs\/pii\/000398616290245X?via%3Dihub\" target=\"_blank\" rel=\"noopener\">10.1016\/0003-9861(62)90245-X<\/a>)<\/span><\/p>\n<p id=\"screen-reader-main-title\" class=\"Head u-font-serif u-h2 u-margin-s-ver\"><span class=\"title-text\"><a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S1047847718303149?via%3Dihub\" target=\"_blank\" rel=\"noopener\">Structural insights into thermostabilization of leucinedehydrogenase from its atomic structure by cryo-electron microscopy<\/a> (By Hiroki Yamaguchi, Akiko Kamegawa, et al; 2019;\u00a0<em>Journal of Structal Biology,\u00a0<\/em>Volume 205, Issue 1, January 2019, Pages 11-21; DOI: <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S1047847718303149?via%3Dihub\" target=\"_blank\" rel=\"noopener\">10.1016\/j.jsb.2018.12.001<\/a>)<\/span><\/p>\n<\/div>","protected":false},"excerpt":{"rendered":"<p>L-Leucin: NAD<sup>+\u00a0<\/sup>oxidoreductase, EC 1.4.1.9<\/p>\n<p>&nbsp;<\/p>\n<p>Synthesen von L-Leucin u.a. Aminos\u00e4uren<\/p>","protected":false},"featured_media":572,"template":"","meta":[],"product_cat":[24],"product_tag":[],"class_list":{"0":"post-449","1":"product","2":"type-product","3":"status-publish","4":"has-post-thumbnail","6":"product_cat-special-enzymes","7":"product_shipping_class-specialenzymes","9":"first","10":"instock","11":"taxable","12":"shipping-taxable","13":"purchasable","14":"product-type-variable"},"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v22.8 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>L-leucine-dehydrogenase - ASA Spezialenzyme GmbH<\/title>\n<meta name=\"description\" content=\"L-leucine-dehydrogenase catalyses the oxidative deamination of L-leucine, L-valine, L-isoleucine and amino acids with unbranched-chained aliphatic carbon.\" \/>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/asa-enzyme.de\/de\/produkt\/l-leucine-dehydrogenase\/\" \/>\n<meta property=\"og:locale\" content=\"de_DE\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"L-leucine-dehydrogenase - 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