Binds Fe2+. The enzyme isolated from the bacterium Pseudomonas sp. 42A2 has similar activity with all the three Delta9 fatty acids. cf. EC 1.13.11.62, linoleate 10R-lipoxygenase.
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SYSTEMATIC NAME
IUBMB Comments
oleate:oxygen (10S)-oxidoreductase
Binds Fe2+. The enzyme isolated from the bacterium Pseudomonas sp. 42A2 has similar activity with all the three Delta9 fatty acids. cf. EC 1.13.11.62, linoleate 10R-lipoxygenase.
enzyme Np-diox is best described as an oleate or linoleate dioxygenase, albeit with alpha-linolenic acid very competitive at low substrate concentrations
the activity of the enzyme is highest in unsaturated fatty acids containing double bonds in position 9 (oleic, linoleic and linolenic acids), linoleic acid being preferred over linolenic and oleic acids
the activity of the enzyme is highest in unsaturated fatty acids containing double bonds in position 9 (oleic, linoleic and linolenic acids), linoleic acid being preferred over linolenic and oleic acids
the enzyme is potently inhibited by 8,10,12- and 9,11,13-conjugated linoleic acid derivatives, found as impurities in the linoleic acid preparation from plant, overview
linoleate 10S-dioxygenase is an ancient relative of cyclooxygenase in cyanobacteria, linoleate 10S-dioxygenase works in tandem with a catalase-related protein with specific 10S-hydroperoxide lyase activity. Neighboring cyanobacterial genes, dioxygenase and catalase, are identified as linoleate 10S-dioxygenase and 10Shydroperoxide lyase, respectively. The Nostoc linoleate 10S-dioxygenase, the sequence of which contains the signature catalytic sequence of cyclooxygenases and fungal linoleate dioxygenases (YRWH), appears to be a heme dioxygenase ancestor
the immediate downstream gene, Np-cat, encodes a specific linoleate 10S-hydroperoxide lyase (10S-hydroperoxyoleate being metabolized at only 3% of the rate) converting the product of Np-diox and working in tandem with it
enzyme Np-diox is an oleate and linoleate heme 10S-dioxygenase-alpha-linolenate is also efficiently metabolized at lower concentrations, but it much more rapidly leads to enzyme inactivation
optimization of conditions for 10S-hydroxy-8(E)-octadecenoic acid production from oleic acid by recombinant Escherichia coli cells expressing Nostoc punctiforme 10S-dioxygenase with the aid of a chaperone plasmid. Optimal conditions are pH 9.0, 35°C, 15 % v/v dimethyl sulfoxide, 40 g cells/l, and 10 g oleic acid/l. The activity of recombinant cells expressing 10S-dioxygenase is increased by 200% with the aid of chaperone Gro7. Production of 10S-hydroxy-8(E)-octadecenoic acid, 10S-hydroxy-8,12(E,Z)-octadecadienoic acid, and 10S-hydroxy-8,12,15(E,Z,Z)-octadecatrienoic acid from unsaturated fatty acids including oleic acid, linoleic acid, and a-linolenic acid, respectively. The soluble 10S-dioxygenase content in the crude extract of recombinant cells co-expressing the 10S-dioxygenase gene with pGro7 is higher than that of recombinant cells co-expressing pKJE7 or pG-KJE8. Production of 360 mg/g/h 10S-hydroxy-8(E)-octadecenoic acid from oleic acid
Busquets, M.; Deroncel, V.; Vidal-Mas, J.; Rodrguez, E.; Guerrero, A.; Manresa, A.
Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid
Martinez, E.; Hamberg, M.; Busquets, M.; Diaz, P.; Manresa, A.; Oliw, E.H.
Biochemical characterization of the oxygenation of unsaturated fatty acids by the dioxygenase and hydroperoxide isomerase of Pseudomonas aeruginosa 42A2
Production of 10S-hydroxy-8(E)-octadecenoic acid from oleic acid by whole recombinant Escherichia coli cells expressing 10S-dioxygenase from Nostoc punctiforme PCC 73102 with the aid of a chaperone
Brash, A.R.; Niraula, N.P.; Boeglin, W.E.; Mashhadi, Z.
An ancient relative of cyclooxygenase in cyanobacteria is a linoleate 10S-dioxygenase that works in tandem with a catalase-related protein with specific 10S-hydroperoxide lyase activity
Rontani, J.; Smik, L.; Vaultier, F.; Widdicombe, C.; Belt, S.
Seasonal monitoring of lipid degradation processes in the western English Channel links bacterial 10S-DOX enzyme activity to free fatty acid production by phytoplankton