Copper is a Cofactor of the Formylglycine‐Generating Enzyme
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Gunnar Jeschke | G. Jeschke | M. Knop | F. Seebeck | Florian P Seebeck | Matthias Knop | Thanh Quy Dang | T. Dang
[1] A. G. Wedd,et al. Unification of the Copper(I) Binding Affinities of the Metallo-chaperones Atx1, Atox1, and Related Proteins , 2011, The Journal of Biological Chemistry.
[2] M. Rudolph,et al. Probing the oxygen-binding site of the human formylglycine-generating enzyme using halide ions. , 2007, Acta crystallographica. Section D, Biological crystallography.
[3] T. Selmer,et al. A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency , 1995, Cell.
[4] M. Marletta,et al. Cellulose degradation by polysaccharide monooxygenases. , 2015, Annual review of biochemistry.
[5] C. Cramer,et al. Effects of thioether substituents on the O2 reactivity of beta-diketiminate-Cu(I) complexes: probing the role of the methionine ligand in copper monooxygenases. , 2006, Journal of the American Chemical Society.
[6] C. Cramer,et al. Isotopic probing of molecular oxygen activation at copper(I) sites. , 2007, Journal of the American Chemical Society.
[7] K. Karlin,et al. A N3S(thioether)-ligated Cu(II)-superoxo with enhanced reactivity. , 2015, Journal of the American Chemical Society.
[8] M. Kubo,et al. Mononuclear copper(II)-superoxo complexes that mimic the structure and reactivity of the active centers of PHM and DbetaM. , 2009, Journal of the American Chemical Society.
[9] T. Dierks,et al. Eukaryotic formylglycine‐generating enzyme catalyses a monooxygenase type of reaction , 2015, The FEBS journal.
[10] Y. Moro-oka,et al. A Monomeric Side-On Superoxocopper(II) Complex: Cu(O2)(HB(3-tBu-5-iPrpz)3) , 1994 .
[11] C. Cramer,et al. Snapshots of dioxygen activation by copper: the structure of a 1:1 Cu/O(2) adduct and its use in syntheses of asymmetric Bis(mu-oxo) complexes. , 2002, Journal of the American Chemical Society.
[12] M. Orio,et al. Side-on cupric-superoxo triplet complexes as competent agents for H-abstraction relevant to the active site of PHM. , 2015, Chemical communications.
[13] Catalina Carrasco-Pozo,et al. Cu(I)-glutathione complex: a potential source of superoxide radicals generation. , 2008, Bioorganic & medicinal chemistry.
[14] Jamie H. D. Cate,et al. Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa. , 2011, ACS chemical biology.
[15] Benjamin F. Gherman,et al. Dioxygen activation at a single copper site: structure, bonding, and mechanism of formation of 1:1 Cu-O2 adducts. , 2004, Journal of the American Chemical Society.
[16] R. Beinart,et al. Thermodynamics and Kinetics of Sulfide Oxidation by Oxygen: A Look at Inorganically Controlled Reactions and Biologically Mediated Processes in the Environment , 2011, Front. Microbio..
[17] Carolyn R Bertozzi,et al. Formylglycine, a post-translationally generated residue with unique catalytic capabilities and biotechnology applications. , 2015, ACS chemical biology.
[18] Adriana Badarau,et al. Copper trafficking mechanism of CXXC-containing domains: insight from the pH-dependence of their Cu(I) affinities. , 2011, Journal of the American Chemical Society.
[19] T. Dierks,et al. Molecular Basis for Multiple Sulfatase Deficiency and Mechanism for Formylglycine Generation of the Human Formylglycine-Generating Enzyme , 2005, Cell.
[20] Donald Hilvert,et al. Minimale Umgestaltung aktiver Enzymtaschen – wie man alten Enzymen neue Kunststücke beibringt , 2007 .
[21] D. Root,et al. Spectroscopic and electronic structure studies of the diamagnetic side-on CuII-superoxo complex Cu(O2)[HB(3-R-5-iPrpz)3]: antiferromagnetic coupling versus covalent delocalization. , 2003, Journal of the American Chemical Society.
[22] Tim Pat Coogan. The I.R.A. , 1970 .
[23] J. Klinman. The Copper-Enzyme Family of Dopamine β-Monooxygenase and Peptidylglycine α-Hydroxylating Monooxygenase: Resolving the Chemical Pathway for Substrate Hydroxylation* , 2006, Journal of Biological Chemistry.
[24] M. Knop,et al. In Vitro Reconstitution of Formylglycine‐Generating Enzymes Requires Copper(I) , 2015, Chembiochem : a European journal of chemical biology.
[25] Donald Hilvert,et al. Minimalist active-site redesign: teaching old enzymes new tricks. , 2007, Angewandte Chemie.
[26] L. Torrance,et al. Unusual Features of Pomoviral RNA Movement , 2011, Front. Microbio..
[27] C. Cramer,et al. An anionic, tetragonal copper(II) superoxide complex. , 2010, Journal of the American Chemical Society.
[28] S. Prigge,et al. Dioxygen Binds End-On to Mononuclear Copper in a Precatalytic Enzyme Complex , 2004, Science.
[29] F. Hollfelder,et al. A new member of the alkaline phosphatase superfamily with a formylglycine nucleophile: structural and kinetic characterisation of a phosphonate monoester hydrolase/phosphodiesterase from Rhizobium leguminosarum. , 2008, Journal of molecular biology.
[30] Torsten Schwede,et al. BIOINFORMATICS Bioinformatics Advance Access published November 12, 2005 The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling , 2022 .
[31] R. Huxtable. Thiols, Disulfides, and Thioesters , 1986 .
[32] A. Ballabio,et al. The Multiple Sulfatase Deficiency Gene Encodes an Essential and Limiting Factor for the Activity of Sulfatases , 2003, Cell.
[33] R. Raines,et al. A Potent, Versatile Disulfide-Reducing Agent from Aspartic Acid , 2012, Journal of the American Chemical Society.
[34] K. Karlin,et al. Cupric superoxo-mediated intermolecular C-H activation chemistry. , 2011, Journal of the American Chemical Society.
[35] Patrick L. Holland,et al. β-Diketiminate ligand backbone structural effects on Cu(I)/O2 reactivity: Unique copper-superoxo and bis(μ-oxo) complexes , 2002 .
[36] T. O’Halloran,et al. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. , 1999, Science.
[37] J. Berger,et al. Function and Structure of a Prokaryotic Formylglycine-generating Enzyme*S⃞ , 2008, Journal of Biological Chemistry.
[38] R. Mains,et al. The catalytic role of the copper ligand H172 of peptidylglycine alpha-hydroxylating monooxygenase (PHM): a spectroscopic study of the H172A mutant. , 2002, Biochemistry.
[39] T. Dierks,et al. Multiple Sulfatase Deficiency Is Caused by Mutations in the Gene Encoding the Human Cα-Formylglycine Generating Enzyme , 2003, Cell.
[40] Carolyn R Bertozzi,et al. Introducing genetically encoded aldehydes into proteins. , 2007, Nature chemical biology.
[41] P. Drake,et al. Reconstitution of Formylglycine-generating Enzyme with Copper(II) for Aldehyde Tag Conversion , 2015, The Journal of Biological Chemistry.
[42] G. G. Stokes. "J." , 1890, The New Yale Book of Quotations.
[43] T. Dierks,et al. A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme. , 2006, Proceedings of the National Academy of Sciences of the United States of America.