Lysosomal Prenylcysteine Lyase Is a FAD-dependent Thioether Oxidase
Open Access
- 1 January 2001
- journal article
- Published by Elsevier
- Vol. 276 (4), 2321-2324
- https://doi.org/10.1074/jbc.c000616200
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- March's Advanced Organic Chemistry: Reactions, Mechanisms, and Structure, 5th EditionMolecules, 2001
- Overexpression of the FAD-binding domain of the sulphite reductase flavoprotein component from Escherichia coli and its inhibition by iodonium diphenyl chlorideBiochemical Journal, 1999
- CaaX converting enzymesCurrent Opinion in Lipidology, 1998
- A Stable Nonfluorescent Derivative of Resorufin for the Fluorometric Determination of Trace Hydrogen Peroxide: Applications in Detecting the Activity of Phagocyte NADPH Oxidase and Other OxidasesAnalytical Biochemistry, 1997
- Lipid thioesters derived from acylated proteins accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase.Proceedings of the National Academy of Sciences, 1996
- Chemical biology of protein isoprenylation/methylationBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1996
- Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosisNature, 1995
- Protein Lipidation in Cell SignalingScience, 1995
- [2] Isolation of protein prenyltransferases from bovine brain and baculovirus expression systemMethods in Enzymology, 1995
- p21ras is modified by a farnesyl isoprenoid.Proceedings of the National Academy of Sciences, 1989