1.13.11.61: linolenate 9R-lipoxygenase

This is an abbreviated version!
For detailed information about linolenate 9R-lipoxygenase, go to the full flat file.

Reaction

Synonyms

(9R)-LOX, 11R-LOX, 9R-lipoxygenase, 9R-LOX, ARA 11RLOX, arachidonate 11R-lipoxygenase, CspLOX2, LA 9RLOX, linoleate 11R-lipoxygenase, linoleate 9R-dioxygenase, lipoxygenase 2, NspLOX

ECTree

     1 Oxidoreductases

         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

             1.13.11 With incorporation of two atoms of oxygen

                1.13.11.61 linolenate 9R-lipoxygenase

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Results	in table
9	Activating Compound
7	AA Sequence
5	Cloned(Commentary)
1	Cofactor
1	Crystallization (Commentary)
1	General Information
11	Inhibitors
6	kcat/KM [mM/s]
12	KM Value [mM]
1	Metals/Ions
2	Molecular Weight [Da]
11	Natural Substrates/ Products (Substrates)
29	Organism
1	Pathway
4	pH Optimum
2	pH Range
9	Protein Variants
4	Purification (Commentary)
2	Reaction
9	Reference
1	Source Tissue
6	Specific Activity [micromol/min/mg]
30	Substrates and Products (Substrate)
4	Subunits
23	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Range [°C]
6	Turnover Number [1/s]

Engineering

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Engineering on EC 1.13.11.61 - linolenate 9R-lipoxygenase

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

A162G

Nostoc sp.

-

the recombinant carboxy-terminal domain of the wild-type enzyme and of mutant enzyme A162G produce primarily (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate from linoleate. The stereochemistry of the hydroperoxide is almost exclusively R (93-94%)

716450

A162I

Nostoc sp.

-

the recombinant carboxy-terminal domain of the mutant enzyme A162I produces almost exlusively (13S)-hydroperoxy octadecadienoic acid (90%)

716450

A162V

Nostoc sp.

-

the recombinant carboxy-terminal domain of the mutant enzyme A162V converts linoleate primarily to (13S)-hydroperoxy octadecadienoic acid (64%) and to a lesser extent to (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate (36%)

716450

A162G

Nostoc sp. PCC 7120

-

the recombinant carboxy-terminal domain of the wild-type enzyme and of mutant enzyme A162G produce primarily (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate from linoleate. The stereochemistry of the hydroperoxide is almost exclusively R (93-94%)

-

A162I

Nostoc sp. PCC 7120

-

the recombinant carboxy-terminal domain of the mutant enzyme A162I produces almost exlusively (13S)-hydroperoxy octadecadienoic acid (90%)

-

A162V

Nostoc sp. PCC 7120

-

the recombinant carboxy-terminal domain of the mutant enzyme A162V converts linoleate primarily to (13S)-hydroperoxy octadecadienoic acid (64%) and to a lesser extent to (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate (36%)

-

G401A

Rippkaea orientalis PCC 8801

-

site-directed mutagenesis, the mutaant shows increased formation of 11-hydroperoxyoctadeca-9,12-dienoate compared to the wild-type enzyme

743826

I617L

Rippkaea orientalis PCC 8801

-

site-directed mutagenesis, the mutaant shows increased formation of 11-hydroperoxyoctadeca-9,12-dienoate compared to the wild-type enzyme

743826

additional information

Rippkaea orientalis PCC 8801

-

Decreasing the channel size of a 9R-lipoxygenase (CspLOX1) can in turn induce formation of the bis-allylic 11R-hydroperoxide

743826