Research Topics
| E K JaffeSummaryAffiliation: Fox Chase Cancer Center Country: USA Publications
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Detail Information
Publications
An artificial gene for human porphobilinogen synthase allows comparison of an allelic variation implicated in susceptibility to lead poisoningE K Jaffe
Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111, USA
J Biol Chem 275:2619-26. 2000..However, there was no differential displacement of Zn(II) by Pb(II) between K59 and N59, and simple Pb(II) inhibition studies revealed no allelic difference...
Characterization of the role of the stimulatory magnesium of Escherichia coli porphobilinogen synthaseE K Jaffe
Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111
Biochemistry 34:244-51. 1995..The addition of unlabeled or 1-13C-labeled ALA does not significantly affect the Mn(II) EPR spectra.(ABSTRACT TRUNCATED AT 250 WORDS)..
Mechanistic implications of mutations to the active site lysine of porphobilinogen synthaseL W Mitchell
Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111, USA
J Biol Chem 276:1538-44. 2001..Thus, formation of the lysine to ALA Schiff base is not required to initiate the asymmetry that results in half-site reactivity...
Mechanistic basis for suicide inactivation of porphobilinogen synthase by 4,7-dioxosebacic acid, an inhibitor that shows dramatic species selectivityJ Kervinen
Institute for Cancer Research, Fox Chase Cancer Center, 7701 Burholme Avenue, Philadelphia, Pennsylvania 19111, USA
Biochemistry 40:8227-36. 2001..coli numbering). This is the first structure to show inhibitor binding at the second of two substrate-binding sites...
The molecular mechanism of lead inhibition of human porphobilinogen synthaseE K Jaffe
Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111, USA
J Biol Chem 276:1531-7. 2001..The data support a novel model where a high affinity lead site is a hybrid of the ZnA and ZnB sites. We propose that the lone electron pair of Pb(II) precludes Pb(II) to function in PBGS catalysis...
13C NMR studies of the enzyme-product complex of Bacillus subtilis chorismate mutaseJ S Rajagopalan
Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111
Biochemistry 32:3965-72. 1993..abstract truncated at 250 words)..
Porphobilinogen synthase from Escherichia coli is a Zn(II) metalloenzyme stimulated by Mg(II)L W Mitchell
Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111
Arch Biochem Biophys 300:169-77. 1993..Li, and M. P. Timko (1991) J. Biol. Chem. 266, 17060-17066]. This work lays the foundation for identification of functional amino acids based on the sequence similarities between PBGS from bacterial, plant, and mammalian sources...
