Fatty acyl coupled catalase |
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| Institution: | 1. Department of Molecular Physiology, Leiden Institute of Chemistry, Leiden University, the Netherlands;2. Laboratory of Cardiovascular Physiology and Tissue Injury, National Institutes of Health/NIAAA, Bethesda, USA;3. Department of Pharmacology and Pharmacotherapy, Faculty of Medicine, Semmelweis University, Budapest, Hungary;4. HCEMM-SU Cardiometabolic Immunology Research Group, Semmelweis University, Budapest, Hungary;5. Department of Analytical Biosciences, Leiden Academic Centre for Drug Research, Leiden University, the Netherlands;6. Department of Heart Failure and Transplantology, Cardinal Stefan Wyszyński Institute of Cardiology, Warszawa, Poland;7. Pharmahungary Group, Szeged, Hungary;1. Dipartimento di Chimica e Chimica Industriale, Via Giuseppe Moruzzi, 13, 56124 Pisa, Italy;2. Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saul?tekio 7, Vilnius LT-10257, Lithuania;3. Department of Bioinformatics, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saul?tekio 7, Vilnius LT-10257, Lithuania;1. Department of Chemistry & Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA;2. Howard Hughes Medical Institute, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA;1. Institute for Molecular Microbiology and Biotechnology, University of Münster, Corrensstraße 3, 48149 Münster, Germany;2. Center for Structural Studies, Heinrich-Heine-University, Universitätsstraße 1, 40225 Düsseldorf, Germany;3. Organic Chemistry Institute, University of Münster, Corrensstraße 40, 48149 Münster, Germany;4. Organic Chemistry Research Group, Department of Chemistry and Department of Bioengineering Sciences, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussel, Belgium;5. Institute of Biochemistry, Heinrich-Heine-University, Universitätsstraße 1, 40225 Düsseldorf, Germany;1. Department of Chemistry, University of Iowa, Iowa City, IA 52242-1294, USA;2. Department of Internal Medicine, University of Nebraska Medical Center, Omaha, NE 68198, USA;3. Department of Pharmacology, University of Iowa, Iowa City, IA 52242-1109, USA |
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| Abstract: | Bovine liver catalase (hydrogen-peroxide:hydrogen peroxide oxidoreductase, EC 1.11.1.6) was derivatized by 9″(10″)-4′-{2-(4,6-dichloro-1,3,5-triazinyl)oxy}butoxy]stearic acid and the fatty acyl-coated enzyme was separated from native catalase and excess reagent by hydroxyapatite chromatography. The derivatization of catalase resulted in coupling the long-chain fatty acyl residues to lysine, histidine and arginine, while other amino acids remained essentially unaffected. The fatty acyl-coated enzyme was water soluble at pH > 7.0 but became octanol and ether soluble at pH < 6.5. The derivatized enzyme retained 50–80% of the catalatic- and peroxidative-specific activities. The free carboxyl function of the coupled long-chain fattyl acyl residues could serve as substrate for ATP-dependent CoA-thioesterification catalyzed by the rat liver microsomal long-chain fatty acyl-CoA synthase. |
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