Probing the Substrate Alignment at the Active Site of 15-Lipoxygenases by Targeted Substrate Modification and Site-Directed Mutagenesis. Evidence for an Inverse Substrate Orientation
- 10 October 1998
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 37 (44) , 15327-15335
- https://doi.org/10.1021/bi9816204
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- Burying a chargeNature Structural & Molecular Biology, 1998
- Structure of soybean lipoxygenase L3 and a comparison with its L1 isoenzymeProteins-Structure Function and Bioinformatics, 1997
- Phenylalanine 353 is a Primary Determinant for the Positional Specificity of Mammalian 15-LipoxygenasesJournal of Molecular Biology, 1996
- The Three-Dimensional Structure of an Arachidonic Acid 15-LipoxygenaseScience, 1993
- Oxygenation of lipoproteins by mammalian lipoxygenasesEuropean Journal of Biochemistry, 1993
- Formation of lipoxin B by the pure reticulocyte lipoxygenase via sequential oxygenation of the substrateEuropean Journal of Biochemistry, 1987
- A kinetic model for lipoxygenases based on experimental data with the lipoxygenase of reticulocytesEuropean Journal of Biochemistry, 1987
- Requirement of monohydroperoxy fatty acids for the oxygenation of 15Ls‐HETE by reticulocyte lipoxygenaseFEBS Letters, 1986
- The Steady-State Kinetics of the Oxygenation of Linoleic Acid Catalysed by Soybean LipoxygenaseEuropean Journal of Biochemistry, 1976