1.14.14.58: trimethyltridecatetraene synthase

This is an abbreviated version!
For detailed information about trimethyltridecatetraene synthase, go to the full flat file.

Reaction

Synonyms

At3g25180, CYP82G1, CYP92C5, CYP92C6, cytochrome P450 82G1, DMNT homoterpene synthase, DMNT synthase, DMNT/TMTT homoterpene synthase, TMTT homoterpene synthase, TMTT synthase

ECTree

     1 Oxidoreductases

         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

             1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor

                1.14.14.58 trimethyltridecatetraene synthase

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Results	in table
5	AA Sequence
4	Cloned(Commentary)
4	Cofactor
2	Crystallization (Commentary)
6	Expression
11	General Information
2	Inhibitors
3	kcat/KM [mM/s]
10	KM Value [mM]
2	Localization
11	Natural Substrates/ Products (Substrates)
10	Organism
3	Pathway
1	Protein Variants
2	Reaction
6	Reference
14	Source Tissue
20	Substrates and Products (Substrate)
21	Synonyms
1	Systematic Name
5	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.14.14.58 - trimethyltridecatetraene synthase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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

Arabidopsis thaliana

Q9LSF8

746284

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

Arabidopsis thaliana

Q9LSF8

713423