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EC Number	Crystallization (Commentary)
1.14.14.58	modeling and substrate docking support an oxidative bond cleavage of the alcohol substrate via syn-elimination of the polar head, together with an allylic C-5 hydrogen atom
1.14.14.58	molecular docking of (E,E)-geranyllinalool and (E)-nerolidol shows that both substrates occupiy the same position in the enzyme binding site with the hydroxyl group at C-3, forming a strong hydrogen bond to the carbonyl oxygen of Thr313. The position of the allylic hydrogen atoms at C-5 of (E,E)-geranyllinalool and (E)-nerolidol and the hydroxyl group at C-3 relative to the reactive iron-oxo heme moiety supports an oxidative-bond cleavage reaction proceeding by a syn-elimination mechanism

EC Number

Crystallization (Commentary)

1.14.14.58

modeling and substrate docking support an oxidative bond cleavage of the alcohol substrate via syn-elimination of the polar head, together with an allylic C-5 hydrogen atom

1.14.14.58

molecular docking of (E,E)-geranyllinalool and (E)-nerolidol shows that both substrates occupiy the same position in the enzyme binding site with the hydroxyl group at C-3, forming a strong hydrogen bond to the carbonyl oxygen of Thr313. The position of the allylic hydrogen atoms at C-5 of (E,E)-geranyllinalool and (E)-nerolidol and the hydroxyl group at C-3 relative to the reactive iron-oxo heme moiety supports an oxidative-bond cleavage reaction proceeding by a syn-elimination mechanism

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Release 2023.1 (January 2023)