Literature summary for 1.13.11.31 extracted from

Reddy, R.G.; Yoshimoto, T.; Yamamoto, S.; Funk, C.D.; Marnett, L.J.
Expression of porcine leukocyte 12-lipoxygenase in a baculovirus/insect cell system and its characterization (1994), Arch. Biochem. Biophys., 312, 219-226.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in insect cells using a baculovirus expression vector, expression as an N-terminal fusion protein with a 31-amino acid polypeptide carrying a six-histidine tag and an enterokinase cleavage site	Sus scrofa

Inhibitors

Inhibitors	Comment	Organism	Structure
5,8,11,14-Eicosatetraynoic acid	IC50: 0.00006 mM	Sus scrofa
nordihydroguaiaretic acid	IC50: 0.0022 mM	Sus scrofa

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.022	-	arachidonic acid	-	Sus scrofa
0.03	-	linoleic acid	-	Sus scrofa

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Sus scrofa

Source Tissue

Source Tissue	Comment	Organism	Textmining
leukocyte	-	Sus scrofa	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.033	-	-	Sus scrofa

Storage Stability

Storage Stability	Organism
-70°C, 20% glycerol, 10 mM 2-mercaptoethanol, 0.3% Triton X-305, enzyme retains complete activity after 1 month	Sus scrofa

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
arachidonate + O2	i.e. 5Z,8Z,11Z,14Z-eicosatetraenoic acid	Sus scrofa	(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate	the 12-(S)-enantiomer is the predominant product	?
linoleic acid + O2	19% of the activity with arachidonic acid	Sus scrofa	13(S)-hydroperoxy-9Z,11E-octadecadienoic acid	-	?

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.00006	-	IC50: 0.00006 mM	Sus scrofa	5,8,11,14-Eicosatetraynoic acid
0.0022	-	IC50: 0.0022 mM	Sus scrofa	nordihydroguaiaretic acid

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Release 2023.1 (January 2023)