1.13.11.40: arachidonate 8-lipoxygenase

This is an abbreviated version!
For detailed information about arachidonate 8-lipoxygenase, go to the full flat file.

Reaction

Synonyms

8(R)-lipoxygenase, 8-lipoxygenase, 8-LOX, 8R-lipoxygenase, 8R-LOX, 8S-lipoxygenase, 8S-LOX, allene oxide synthase-lipoxygenase protein, arachidonic acid C-8 lipoxygenase, eicosapentaenoic 8R-lipoxygenase, LOX-1, More

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

                1.13.11.40 arachidonate 8-lipoxygenase

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All data fields related to EC 1.13.11.40

Results	in table
2	Activating Compound
7	AA Sequence
2	Application
1	CAS Registry Number
11	Cloned(Commentary)
5	Crystallization (Commentary)
4	General Information
2	General Stability
7	Inhibitors
4	kcat/KM [mM/s]
17	KM Value [mM]
3	Localization
4	Metals/Ions
2	Molecular Weight [Da]
15	Natural Substrates/ Products (Substrates)
22	Organism
4	Pathway
20	PDB ID
5	pH Optimum
1	pH Range
1	Posttranslational Modification
26	Protein Variants
9	Purification (Commentary)
1	Reaction
4	Reaction Type
22	Reference
7	Source Tissue
2	Specific Activity [micromol/min/mg]
3	Storage Stability
51	Substrates and Products (Substrate)
2	Subunits
22	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
1	Temperature Range [°C]
17	Turnover Number [1/s]

General Information

General Information on EC 1.13.11.40 - arachidonate 8-lipoxygenase

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

metabolism

Plexaura homomalla

O16025

the mechanism consists of hydrogen abstraction from one double allylic carbon atom of substrate followed by oxygen insertion at the resulting prochiral carbon radical of the substrate. The positional specificity of the hydrogen abstraction is a result of conformational dynamics of the bound substrate. The C10 atom of the substrate is the most probable site of hydrogen abstraction in wild-type. The dominating 8R product in the wild-type is due to the presence of the aromatic ring pairs of Tyr181 and Phe173 acting as a gatekeeper for efficient delivery of oxygen at the pro-R face of C8

765268

physiological function

Plexaura homomalla

-

lipoxygenases (LOXs) are a family of enzymes that catalyze the highly specific hydroperoxidation of polyunsaturated fatty acids, such as arachidonic acid. Different stereo- or/and regioisomer hydroperoxidation products lead later to different metabolites that exert opposite physiological effects in the animal body and play a central role in inflammatory processes. The Gly-Ala switch of a single residue is crucial for the stereo- and regiocontrol in many lipoxygenases

741487

additional information

2 entries

additional information

Plexaura homomalla

-

molecular dynamics simulations, quantum mechanics/molecular mechanics calculations, overview. In wild-type, molecular oxygen adds to C8 of arachidonic acid with an R stereochemistry. In the mutant, Ala427 pushes Leu385, blocks the region over C8, and opens an oxygen access channel now directed to C12, where molecular oxygen is added with an S stereochemistry. Thus, the specificity turns out to be dramatically inverted

741487

additional information

Plexaura homomalla

O16025

subtle rearrangements, primarily in the side chains of three amino acids, allow binding of arachidonic acid in a catalytically competent conformation, both substrate tethering and cavity depth contribute to positioning the appropriate carbon at the catalytic machinery, modeling, overview

742865