Literature summary for 4.2.1.92 extracted from

Lee, D.; Nioche, P.; Hamberg, M.; Raman, C.S.
Structural insights into the evolutionary paths of oxylipin biosynthetic enzymes (2008), Nature, 455, 363-368.

Search for more literature for 4.2.1.92

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment)	Organism
AOS free or in complex with 12R,13S-vernolic acid, sitting drop vapour diffusion method, using 100 mM Tris-HCl, pH 7.5, 15-20% polyethylene glycol 3350, and 39 mM nonanoyl-N-hydroxyethylglucamide	Arabidopsis thaliana

Protein Variants

Protein Variants	Comment	Organism
F137L	the mutant is severely compromised in its ability to generate allene oxide and exhibits robust hydroperoxide lyase activity	Arabidopsis thaliana
F137L/S155A	the double mutant exhibits strong hydroperoxide lyase activity	Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q96242	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni-NTA column chromatography	Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid	-	Arabidopsis thaliana	(12S,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O	-	?

Synonyms

Synonyms	Comment	Organism
allene oxide synthase	-	Arabidopsis thaliana
AOS	-	Arabidopsis thaliana
CYP74A	-	Arabidopsis thaliana

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Release 2023.1 (January 2023)