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36747-82-7

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36747-82-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 36747-82-7 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,6,7,4 and 7 respectively; the second part has 2 digits, 8 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 36747-82:
(7*3)+(6*6)+(5*7)+(4*4)+(3*7)+(2*8)+(1*2)=147
147 % 10 = 7
So 36747-82-7 is a valid CAS Registry Number.

36747-82-7Downstream Products

36747-82-7Relevant articles and documents

Highly terminal-selective epoxidation of linolenic acid with an amphiphilic iron porphyrin catalyst casted in bilayer membranes

Naruta, Yoshinori,Goto, Masa-oki,Tawara, Toshifumi,Tani, Fumito

, p. 162 - 163 (2002)

An amphiphilic iron porphyrin having four hexadecanoic acid chains on each face of the porphyrin was prepared and the catalytic epoxidation of linolenic acid with the heme-casted bilayer membranes was achieved in high regioselectivity at the terminal doub

Replacement of two amino acids of 9R-dioxygenase-allene oxide synthase of Aspergillus niger inverts the chirality of the hydroperoxide and the allene oxide

Sooman, Linda,Wennman, Anneli,Hamberg, Mats,Hoffmann, Inga,Oliw, Ernst H.

, p. 108 - 118 (2016/01/08)

The genome of Aspergillus niger codes for a fusion protein (EHA25900), which can be aligned with ~50% sequence identity to 9S-dioxygenase (DOX)-allene oxide synthase (AOS) of Fusarium oxysporum, homologues of the Fusarium and Colletotrichum complexes and with over 62% sequence identity to homologues of Aspergilli, including (DOX)-9R-AOS of Aspergillus terreus. The aims were to characterize the enzymatic activities of EHA25900 and to identify crucial amino acids for the stereospecificity. Recombinant EHA25900 oxidized 18:2n-6 sequentially to 9R-hydroperoxy-10(E),12(Z)-octadecadienoic acid (9R-HPODE) and to a 9R(10)-allene oxide. 9S- and 9R-DOX-AOS catalyze abstraction of the pro-R hydrogen at C-11, but the direction of oxygen insertion differs. A comparison between twelve 9-DOX domains of 9S- and 9R-DOX-AOS revealed conserved amino acid differences, which could contribute to the chirality of products. The Gly616Ile replacement of 9R-DOX-AOS (A. niger) increased the biosynthesis of 9S-HPODE and the 9S(10)-allene oxide, whereas the Phe627Leu replacement led to biosynthesis of 9S-HPODE and the 9S(10)-allene oxide as main products. The double mutant (Gly616Ile, Phe627Leu) formed over 90% of the 9S stereoisomer of HPODE. 9S-HPODE was formed by antarafacial hydrogen abstraction and oxygen insertion, i.e., the original H-abstraction was retained but the product chirality was altered. We conclude that 9R-DOX-AOS can be altered to 9S-DOX-AOS by replacement of two amino acids (Gly616Ile, Phe627Leu) in the DOX domain.

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