Eileen K. Jaffe, PhD-Publications

Peer Reviewed Publications
Published Patents

Peer Reviewed Publications

Lawrence SH, Ramirez UD, Selwood T, Stith L, Jaffe EK. Allosteric inhibition of human porphobilinogen synthase. J Biol Chem. 2009 Dec 18;284(51):35807-17. PubMed
Kokona B, Rigotti DJ, Wasson AS et al. Probing the Oligomeric Assemblies of Pea Porphobilinogen Synthase by Analytical Ultracentrifugation. Biochemistry. 2008;47(40):10649-56. PubMed.
Lawrence SH, Jaffe EK. Expanding the concepts in protein-structure-function relationships and enzyme kinetics: Teaching using morpheeins. Biochem Mol Biol Educ. 2008;36(4):274-83. PubMed.
Lawrence SH, Ramirez UD, Tang L et al. Shape shifting leads to small-molecule allosteric drug discovery. Chem Biol. 2008c;15(6):586-96. PubMed.
Selwood T, Tang L, Lawrence SH et al. Kinetics and thermodynamics of the interchange of the morpheein forms of human porphobilinogen synthase. Biochemistry. 2008;47(10):3245-57. PubMed.
Jaffe EK, Stith L. ALAD porphyria is a conformational disease. Am J Hum Genet. 2007;80(2):329-37. PubMed.
Shenker BJ, Dlakic M, Walker LP et al. A Novel Mode of Action for a Microbial-Derived Immunotoxin: The Cytolethal Distending Toxin Subunit B Exhibits Phosphatidylinositol (3,4,5)-Trisphosphate Phosphatase Activity. J Immunol. 2007;178(8):5099-108. PubMed.
Akagi R, Kato N, Inoue R et al. delta-Aminolevulinate dehydratase (ALAD) porphyria: the first case in North America with two novel ALAD mutations. Mol Genet Metab. 2006;87(4):329-36. PubMed.
Tang L, Breinig S, Stith L et al. Single amino acid mutations alter the distribution of human porphobilinogen synthase quaternary structure isoforms (morpheeins). J Biol Chem. 2006;281(10):6682-90. PubMed.
Cheng JD, Valianou M, Canutescu AA et al. Abrogation of fibroblast activation protein enzymatic activity attenuates tumor growth. Mol Cancer Ther. 2005;4(3):351-60. PubMed.
Jaffe EK. Morpheeins - a new structural paradigm for allosteric regulation. Trends Biochem Sci. 2005;30(9):490-7. PubMed.
Tang L, Stith L, Jaffe EK. Substrate-induced interconversion of protein quaternary structure isoforms. J Biol Chem. 2005;280(16):15786-93. PubMed.
Bollivar DW, Clauson C, Lighthall R et al. Rhodobacter capsulatus porphobilinogen synthase, a high activity metal ion independent hexamer. BMC Biochem. 2004;5:No pp given. PubMed.
Jaffe EK. The porphobilinogen synthase catalyzed reaction mechanism. Bioorg Chem. 2004;32(5):316-25. PubMed.
Breinig S, Kervinen J, Stith L et al. Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase. Nat Struct Biol. 2003;10(9):757-63. PubMed.
Jaffe EK. Investigations on the metal switch region of human porphobilinogen synthase. JBIC, J Biol Inorg Chem. 2003a;8(1-2):176-84. PubMed.
Jaffe EK. An unusual phylogenetic variation in the metal ion binding sites of porphobilinogen synthase. Chem Biol. 2003;10(1):25-34. PubMed.
Kundrat L, Martins J, Stith L et al. A structural basis for half-of-the-sites metal binding revealed in Drosophila melanogaster porphobilinogen synthase. J Biol Chem. 2003;278(33):31325-30. PubMed.
Jaffe EK, Kervinen J, Martins J et al. Species-specific inhibition of porphobilinogen synthase by 4-oxosebacic acid. J Biol Chem. 2002;277(22):19792-9. PubMed.
Jaffe EK, Martins J, Li J et al. The molecular mechanism of lead inhibition of human porphobilinogen synthase. J Biol Chem. 2001;276(2):1531-7. PubMed.
Kervinen J, Jaffe EK, Stauffer F et al. Mechanistic basis for suicide inactivation of porphobilinogen synthase by 4,7-dioxosebacic acid, an inhibitor that shows dramatic species selectivity. Biochemistry. 2001;40(28):8227-36. PubMed.
Mitchell LW, Volin M, Martins J et al. Mechanistic implications of mutations to the active site lysine of porphobilinogen synthase. J Biol Chem. 2001;276(2):1538-44. PubMed.
Jaffe EK. The porphobilinogen synthase family of metalloenzymes. Acta Crystallogr D Biol Crystallogr. 2000;56(Pt 2):115-28. PubMed.
Jaffe EK, Volin M, Bronson-Mullins CR et al. An artificial gene for human porphobilinogen synthase allows comparison of an allelic variation implicated in susceptibility to lead poisoning. J Biol Chem. 2000;275(4):2619-26. PubMed.
Kervinen J, Dunbrack RL, Jr., Litwin S et al. Porphobilinogen synthase from pea: expression from an artificial gene, kinetic characterization, and novel implications for subunit interactions. Biochemistry. 2000;39(30):9018-29. PubMed.
Frankenberg N, Jahn D, Jaffe EK. Pseudomonas aeruginosa Contains a Novel Type V Porphobilinogen Synthase with No Required Catalytic Metal Ions. Biochemistry. 1999;38(42):13976-82. PubMed.
Shimoni-Livny L, Carrell HL, Wagner T et al. Crystallization and preliminary x-ray diffraction studies of E. coli porphobilinogen synthase and its heavy-atom derivatives. Acta Crystallogr, Sect. D: Biol Crystallogr. 1998;D54(3):438-40. PubMed.
Clarkson J, Jaffe EK, Petrovich RM et al. Opportunities for Probing the Structure and Mechanism of Porphobilinogen Synthase by Raman Spectroscopy. J Am Chem Soc. 1997;119(47):11556-7.
Petrovich RM, Jaffe EK. Magnetic Resonance Studies on the Active Site and Metal Centers of Bradyrhizobium japonicum Porphobilinogen Synthase. Biochemistry. 1997;36(43):13421-7. PubMed.
Carrell HL, Glusker JP, Shimoni L et al. Crystallization and preliminary x-ray diffraction studies of 5-chlorolevulinate-modified bovine porphobilinogen synthase and the PbII-complexed enzyme. Acta Crystallogr., Sect. D: Biol Crystallogr. 1996;D52(2):419-21.
Petrovich RM, Litwin S, Jaffe EK. Bradyrhizobium japonicum porphobilinogen synthase uses two Mg(II) and monovalent cations. J Biol Chem. 1996;271(15):8692-9. PubMed.
Jaffe EK. Porphobilinogen synthase, the first source of heme's asymmetry. J Bioenerg Biomembr. 1995;27(2):169-79. PubMed.
Jaffe EK, Ali S, Mitchell LW et al. Characterization of the Role of the Stimulatory Magnesium of Escherichia coli Porphobilinogen Synthase. Biochemistry 1995;34(1):244-51. PubMed.
Jaffe EK, Petrovich RM, Volin M. 5-Chlorolevulinate interactions with Bradyrhizobium japonicum porphobilinogen synthase. Bioorg Chem. 1995;23(4):450-9.
Mitchell LW, Volin M, Jaffe EK. The phylogenetically conserved histidines of Escherichia coli porphobilinogen synthase are not required for catalysis. J Biol Chem. 1995;270 (41):24054-9.
Jaffe EK, Volin M, Myers CB et al. 5-Chloro[1,4-13C]levulinic acid modification of mammalian and bacterial porphobilinogen synthase suggests an active site containing two Zn(II). Biochemistry. 1994;33(38):11554-62. PubMed.
Jaffe EK. Predicting the Zn(II) ligands in metalloproteins: case study, porphobilinogen synthase. Comments Inorg. Chem. 1993;15(2):67-92.
Markham GD, Myers CB, Harris KA, Jr. et al. Spatial proximity and sequence localization of the reactive sulfhydryls of prophobilinogen synthase. Protein Sci. 1993;2(1):71-9. PubMed.
Mitchell LW, Jaffe EK. Porphobilinogen synthase from Escherichia coli is a zinc(II) metalloenzyme stimulated by magnesium(II). Arch Biochem. Biophys. 1993;300(1):169-77. PubMed.
Rajagopalan JS, Jaffe EK. Microbial production and NMR characterization of [2,6,9-13C]chorismate and [1,3,5,8-13C]chorismate. Bioorg. Med. Chem. Lett. 1993; 3 (7):1453-6.
Rajagopalan JS, Taylor KM, Jaffe EK. Carbon-13 NMR studies of the enzyme-product complex of Bacillus subtilis chorismate mutase. Biochemistry 1993b; 32 (15):3965-72.
Afshar C, Jaffe EK, Carrell HL et al. The molecular conformation of chorismic acid in the crystalline state. Bioorg Chem. 1992;20(4):323-33.
Jaffe EK, Abrams WR, Kaempfen HX et al. 5-Chlorolevulinate modification of porphobilinogen synthase identifies a potential role for the catalytic zinc. Biochemistry. 1992;31(7):2113-23. PubMed.
Rajagopalan JS, Chen LC, Jaffe EK. Preparation, carbon-13 NMR characterization, and enzymic transformation of [U-13C]chorismate to [U-13C]prephenate and [U-13C]hydroxyphenyl pyruvate. Bioorg Chem. 1992;20(2):115-23.
Jaffe EK, Bagla S, Michini PA. Reevaluation of a sensitive indicator of early lead exposure: measurement of porphobilinogen synthase in blood. Biol Trace Elem Res. 1991;28(3):223-31. PubMed.
Jaffe EK, Markham GD, Rajagopalan JS. 15N and 13C NMR studies of ligands bound to the 280,000-dalton protein porphobilinogen synthase elucidate the structures of enzyme-bound product and a Schiff base intermediate. Biochemistry. 1990;29 (36):8345-50. PubMed.
Jaffe EK, Rajagopalan JS. Nuclear magnetic resonance studies of 5-aminolevulinate demonstrate multiple forms in aqueous solution. Bioorg Chem. 1990;18(4):381-94.
Jaffe EK, Markham GD. Carbon-13 NMR studies of methylene and methine carbons of substrate bound to a 280,000-dalton protein, porphobilinogen synthase. Biochemistry. 1988;27(12):4475-81.
Jaffe EK, Markham GD. Carbon-13 NMR studies of porphobilinogen synthase: observation of intermediates bound to a 280,000-dalton protein. Biochemistry. 1987;26(14):4258-64.
Jaffe EK, Hanes D. Dissection of the early steps in the porphobilinogen synthase catalyzed reaction. Requirements for Schiff's base formation. J Biol Chem. 1986;261(20):9348-53. PubMed.
Jaffe EK, Salowe SP, Chen NT et al. Porphobilinogen synthase modification with methylmethanethiosulfonate. A protocol for the investigation of metalloproteins. J Biol Chem. 1984;259(8):5032-6. PubMed.
Addadi L, Jaffe EK, Knowles JR. Secondary tritium isotope effects as probes of the enzymic and nonenzymic conversion of chorismate to prephenate. Biochemistry. 1983;22(19):4494-501. PubMed.
Jaffe EK, Nick J, Cohn M. Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity of chromium(III)-ATP in the 3-phosphoglycerate kinase reaction. Structure of the metal nucleotide substrates. J Biol Chem. 1982;257(13):7650-6.
Jaffe EK, Cohn M. Shift of the equilibrium constant of the 3-phosphoglycerate kinase reaction towards 1,3-bis-phosphoglycerate with adenosine 5'-O-(2-thiotriphosphate) (ATPbS) as substrate. J Biol Chem. 1980;255(8):3240-1.
Jaffe EK, Cohn M. Shift of the equilibrium constant of the 3-P-glycerate kinase reaction towards 1,3-bis-P-glycerate with adenosine 5'-O-(2-thiotriphosphate) (ATP beta S) as substrate. J Biol Chem. 1980;255(8):3240-1. PubMed.
Jaffe EK. Adenosine phosphorothioates; phosphorus-31 NMR, and their metal ion dependent stereospecificity in the reactions of hexokinase and other kinases; 1979. 162 pp p.
Jaffe EK, Cohn M. Diastereomers of the nucleoside phosphorothioates as probes of the structure of the metal nucleotide substrates and of the nucleotide binding site of yeast hexokinase. J Biol Chem. 1979;254(21):10839-45. PubMed.
Jaffe EK, Cohn M. Phosphorus-31 nuclear magnetic resonance spectra of the thiophosphate analogs of adenine nucleotides; effects of pH and magnesium(2+) binding. Biochemistry. 1978;17(4):652-7.
Jaffe EK, Cohn M. 31P nuclear magnetic resonance spectra of the thiophosphate analogues of adenine nucleotides; effects of pH and Mg2+ binding. Biochemistry. 1978;17(4):652-7. PubMed.
Jaffe EK, Cohn M. Divalent cation-dependent stereospecificity of adenosine 5'-O-(2-thiotriphosphate) in the hexokinase and pyruvate kinase reactions. The absolute stereochemistry of the diastereoisomers of adenosine 5'-O-(2-thiotriphosphate). J Biol Chem. 1978;253(14):4823-5. PubMed.
Jaffe EK, Zipp AP. Spectroscopic and equilibrium studies of adduct formation between sulfoxides and bis(2,4-pentanedionato)oxovanadium(IV). Journal of Inorganic and Nuclear Chemistry. 1978;40 (5):839-41.
Owen CS, Jaffe EK, Wilson DF. Application of a superconducting susceptometer to biological samples. Rev Sci Instr. 1977;48:1541-4.
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Published Patents

Jaffe EK, inventors; (Fox Chase Cancer Center, USA). assignee. Alternative pathways of conformational change in allosteric proteins as a target for the development of bioactive molecules. Application: US, US patent 2008-142435, 2009048324. 2009 20080619.
Jaffe EK, inventors; (USA). assignee. Alternate quaternary isoforms (morpheeins) of porphobilinogen synthase and other allosteric enzymes as a target for the development of antimicrobials and herbicides. Application: US, US patent 2006-327762, 2006162014. 2006 20060106.
Jaffe EK, inventors; (Fox Chase Cancer Center, USA). assignee. Hexameric porphobilinogen synthase as a target for the development of antibiotics and herbicides. Application: WO, WO patent 2004-US21722, 2005007817. 2005 20040707.
Jaffe EK, inventors; (Fox Chase Cancer Center, USA). assignee. Blood lead diagnostic assay. Application: WO, WO patent 94-US8626, 9504159. 1995 19940802.
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