lipoxygenase Protein, Pseudomonas aeruginosa (FLAG, His)

The lipoxygenase protein catalyzes the oxygen-mediated conversion of linoleic acid to 9HPOD and spontaneously decomposes it into 9HOD. It converts linolenic acid into 13HPOD, which breaks down into 13HOD. lipoxygenase Protein, Pseudomonas aeruginosa (FLAG, His) is the recombinant lipoxygenase protein, expressed by E. coli , with N-6*His, N-Flag labeled tag. The total length of lipoxygenase Protein, Pseudomonas aeruginosa (FLAG, His) is 678 a.a., .

In the presence of oxygen, the lipoxygenase protein catalyzes the conversion of linoleate into (9S)-hydroperoxy-10,12-octadecenoate (9HPOD), with subsequent spontaneous decomposition into the corresponding 9-hydroxy-10,12-octadecenoate (9HOD). It also transforms linolenate into its hydroperoxy derivative, 13-hydroperoxy-9,11-octadecenoate (13HPOD), which spontaneously decomposes to the corresponding 13-hydroxy-9,11-octadecenoate (13HOD). Additionally, the enzyme exhibits activity on oleate, albeit to a lesser extent, converting it into (10S)-hydroperoxy-8E-octadecenoate, which undergoes spontaneous decomposition to form the corresponding 10-hydroxy-8E-octadecenoate. Notably, lipoxygenase demonstrates minimal activity on arachidonate. This enzymatic versatility highlights its role in mediating diverse fatty acid oxygenation reactions, contributing to the intricate metabolic pathways associated with lipid signaling and inflammation.

Others

E. coli

N-6*His;N-Flag

Q8RNT4 (M1-I678)

/

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.