1.14.19.39 linoleate + AH2 + O2 - Caenorhabditis elegans crepenynate + A + 2 H2O - ? 428772 1.14.19.39 linoleate + NAD(P)H + O2 enzyme is involved in biosynthesis of crepenynic acid Crepis alpina crepenynate + NAD(P)+ + H2O - ? 369935 1.14.19.39 linoleate + NADH + O2 - Crepis alpina crepenynate + NAD+ + H2O - ? 186808 1.14.19.39 linoleate + NADPH + O2 - Crepis alpina crepenynate + NADP+ + H2O - ? 186809 1.14.19.39 linoleate + reduced acceptor + O2 - Crepis alpina crepenynate + acceptor + H2O - ? 375174 1.14.19.39 linoleate + reduced acceptor + O2 first committed step in the biosynthesis of fatty acid-derived acetylenic secondary natural products, e.g. matricaria esters Crepis alpina crepenynate + acceptor + H2O - ? 375174 1.14.19.39 linoleate + reduced acceptor + O2 enzyme is equally efficient with linoleate and oleate Crepis alpina crepenynate + acceptor + H2O - ? 375174 1.14.19.39 additional information key enzyme in adaptation to low temperature, sequential changes in fatty acid composition on lowering environmental temperature, overview Acanthamoeba castellanii ? - ? 89 1.14.19.39 additional information substrate specificity, the recombinant enzyme catalyzes also the DELTA15-desaturation of fatty acids, and is capable of producing very unusual n-1 polyunsaturated products, overview Acanthamoeba castellanii ? - ? 89 1.14.19.39 additional information H6Cf0807 is an acetylenase, that produces a trans DELTA12 double bond, while H6Cf0745 is a classical FAD2 desaturase. The Cantharellus formosus FAD2 homologue H6Cf0745 expression results in the production of only 16:2 DELTA9,12 and 18:2 DELTA9,12 in recombinant yeast cells supplemented with 18:2 DELTA9c,12c. Expression ofH6Cf0807 results in the production of crepenynic acid, 18:1 DELTA9c,12a. No C16 acetylenic fatty acid is detected. Supplementation with 18:2 DELTA9c,12t, alpha-linolenic acid, 18:3 DELTA9,12,15, or gamma-linolenic acid, 18:3 DELTA6,9,12, does not result in the production of other fatty acids, overview Cantharellus formosus ? - ? 89 1.14.19.39 additional information the enzyme is able to desaturate C16 and C18 fatty acids. When recombinantly expressed in yeast cells, the enzyme can also catalyze DELTA15 desaturation. The recombinant enzyme can also produce C14:2DELTA9,12, C15:2DELTA9,12, C17:2DELTA9,12, and C18:4DELTA6,9,12,15 when C14:1DELTA9, C15:1DELTA9, C17:1DELTA9, and C18:3DELTA6,9,12 substrates are available in yeast cells, product mass spectrometry analysis Caenorhabditis elegans ? - ? 89 1.14.19.39 oleate + AH2 + O2 oxygenation at the sn-2 position Acanthamoeba castellanii linoleate + A + 2 H2O - ? 398007 1.14.19.39 oleate + AH2 + O2 recombinant enzyme Caenorhabditis elegans linoleic acid + linolenic acid + A + 2 H2O - ? 428858 1.14.19.39 oleate + reduced acceptor + O2 enzyme is equally efficient with linoleate and oleate, via intermediates 9(Z),12(E)-octadecadienoate and 9,12(Z)-octadecadienoate, only the latter of which is further catalysed to give crepenynate, i.e. 9(Z)-octadecen-12-ynoate Crepis alpina crepenynate + acceptor + H2O product enantiomers in a ration of 3:1 ? 377411 1.14.19.39 palmitoleic acid + O2 recombinant enzyme Caenorhabditis elegans hexadecadienoic acid + hexadecatrienoic acid + A + 2 H2O - ? 428863 1.14.19.39 palmitoleoate + AH2 + O2 via intermediate DELTA9,12 hexadecadienoate Acanthamoeba castellanii 9,12,15-hexadecatrienoate + A + H2O the product is n-1 polyunsaturated ? 398056 1.14.19.39 phosphatidylcholine + AH2 + O2 - Acanthamoeba castellanii ? - ? 398118 1.14.19.39 phosphatidylcholine + reduced cytochrome b5 + O2 with NADH Physcomitrium patens ? + cytochrome b5 + 2 H2O - ? 427505