Literature summary extracted from

Rapoport, S.M.; Schewe, T.; Wiesner, R.; Halangk, W.; Ludwig, P.; Janicke-Hoehne, M.; Tannert, C.; Hiebsch, C.; Klatt, D.
The lipoxygenase of reticulocytes. Purification, characterization and biological dynamics of the lipoxygenase; its identity with the respiratory inhibitors of the reticulocyte (1979), Eur. J. Biochem., 96, 545-561.

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
1.13.11.33	Iron	contains 1.76 mol of iron per mol of enzyme	Oryctolagus cuniculus

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.13.11.33	78000	-	sucrose density gradient centrifugation, analytical ultracentrifugation	Oryctolagus cuniculus

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.13.11.33	Oryctolagus cuniculus	-	-	-

Posttranslational Modification

EC Number	Posttranslational Modification	Comment	Organism
1.13.11.33	glycoprotein	contains 4.6% neutral sugar	Oryctolagus cuniculus

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.13.11.33	-	Oryctolagus cuniculus

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
1.13.11.33	reticulocyte	reticulocyte-rich anaemic blood cells	Oryctolagus cuniculus	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.13.11.33	arachidonate + O2	-	Oryctolagus cuniculus	(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)