EC Number   |
General Information |
Reference |
|---|
   1.14.14.39 | physiological function |
bifunctional enzyme, metabolizes L-valine as well as L-isoleucine, i.e. activities of EC 1.14.14.38 and 1.14.14.39, consistent with the cooccurrence of linamarin and lotaustralin in cassava |
708971 |
| 1.14.14.39 | physiological function |
bifunctional enzyme, metabolizes L-valine as well as L-isoleucine, i.e. activities of EC 1.14.14.38 and 1.14.14.39, consistent with the cooccurrence of linamarin and lotaustralin in cassava. CYP79D1 has a higher kcat value with L-valine as substrate than with L-isoleucine, which is consistent with linamarin being the major cyanogenic glucoside in cassava |
708971 |
| 1.14.14.39 | physiological function |
enzyme catalyzes the conversion of Val and Ile to the corresponding aldoximes in biosynthesis of cyanogenic glucosides and nitrile glucosides in Lotus japonicus. Recombinantly expressed isoforms CYP79D3 and CYP79D4 in yeast cells show higher catalytic efficiency with L-Ile as substrate than with L-Val, in agreement with lotaustralin and rhodiocyanoside A and D being the major cyanogenic and nitrile glucosides in Lotus japonicus |
710304 |
| 1.14.14.39 | physiological function |
enzyme is part of the biosynthetic pathway leading to nitrile glucosides rhodiocyanoside A and rhodiocyanoside D as well as the cyanogenic glucosides linamarin and lotaustralin. Lotaustralin, rhodiocyanoside A, and rhodiocyanoside D are derived from the amino acid L-Ile, whereas linamarin is derived from L-Val |
710304 |
