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Literature summary extracted from

  • Mishra, V.K.; Mishra, S.
    Origin of regio- and stereospecific catalysis by 8-lipoxygenase (2019), J. Phys. Chem. B, 123, 10605-10621 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.40 molecular dynamics simulations. The enzyme is stable in both apo and substrate bound complex forms. The substrate adopts a bent structure inside the enzyme active site, with the C1 carboxylate and C20 methyl groups of the substrate at two terminal ends of the two sides, while the substrate is folded at the double allylic carbon center (C10 position) Plexaura homomalla

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.40 A592M stability of the enzyme-substrate complex is similar to wild-type. Contrary to wild-type, hydrogen abstraction from C13 is more favorable in the mutant. A592M yields 19% 8R product, 2% 8S, 60% 11R, 4% 11S, plus some 12R/12S and 15R/15S product Plexaura homomalla
1.13.11.40 A623H stability of the enzyme-substrate complex is similar to wild-type. Contrary to wild-type, hydrogen abstraction from C13 is more favorable in the mutant. A623H yields 16% 8R product, 4% 8S, 57% 11R, 5% 11S, 6% 12R, 6% 12S plus some 15R/15S product Plexaura homomalla
1.13.11.40 R185A stability of the enzyme-substrate complex is similar to wild-type. Contrary to wild-type, hydrogen abstraction from C13 is more favorable in the mutant. R185A yields 87% 8R product, 2% 8S plus some 11R/11S, 12R/12S and 15R/15S product Plexaura homomalla

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.40 Iron during the hydrogen abstraction step, the hydroxyl group bound to the metal center activates the C-H bond of the double-allylic carbon center of the substrate that leads to the formation of a radical center at the substrate Plexaura homomalla

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.40 Plexaura homomalla O16025 bifunctional allene oxide synthase-lipoxygenase protein
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.40 arachidonate + O2
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 Plexaura homomalla (5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
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 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.40 allene oxide synthase-lipoxygenase protein
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 Plexaura homomalla

General Information

EC Number General Information Comment Organism
1.13.11.40 metabolism 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 Plexaura homomalla