Literature summary for 1.13.11.34 extracted from

Gilbert, N.C.; Gerstmeier, J.; Schexnaydre, E.E.; Boerner, F.; Garscha, U.; Neau, D.B.; Werz, O.; Newcomer, M.E.
Structural and mechanistic insights into 5-lipoxygenase inhibition by natural products (2020), Nat. Chem. Biol., 16, 783-790 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with inhibitor nordihydroguaiaretic acid, at 2.71 A resolution. The presence of the inhibitor is incompatible with the closed structure of the enzyme. Structure in complex with inhibitor 3-acetyl-11-keto-beta-boswellic acid at 3.0 A resolution. 3-Acetyl-11-keto-beta-boswellic acid lies lengthwise in a deep groove between the amino-terminal and catalytic domains	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
3-acetyl-11-keto-beta-boswellic acid	allosteric inhibitor from frankincense, wedges between the membrane-binding and catalytic domains of 5-LOX, some 30 A from the catalytic iron. Binding promotes a shift in the regiospecificity, i.e. a significant increase in the formation of 12-hydroxyeicosatetraenoic acid with the most prominent effect at 10 microM	Homo sapiens
nordihydroguaiaretic acid	redox-type inhibitor, is lodged in the 5-LOX active site, fully exposed by disordering of the helix that caps it in the apo-enzyme	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P09917	-	-

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Release 2023.1 (January 2023)