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Title: E. coli porphobilinogen synthase in a Zn(II) metalloenzyme

Conference · · FASEB Journal (Federation of American Societies for Experimental Biology); (United States)
OSTI ID:6894118
;  [1]
  1. Inst. for Cancer Research, Philadelphia, PA (United States)

E. coli porphobilinogen synthase (PBGS) has been purified and characterized. In this vein the authors have determined that E. coli PBGS activity is (1) stimulated by low concentrations of Zn(II); (2) inhibited by excess Zn(II); (3) inhibited by the Zn(II) chelator 1,10-phenanthroline; (4) inactivated by methyl-methanethiosulfonate, a cysteine modifier; and (5) shows exceptional thermal stability. These observations mimic those for bovine PBGS and are not unexpected in lieu of the 38% sequence identify between E. coli and mammalian PBGS. The authors have previously used [sup 13]C NMR to characterize the enzyme-product complex for bovine PBGS; the signals from bound porphobilinogen (PBG) are distinct from those of free PBG and indicate deprotonation of the product amine group. Similar experiments with E. coli PBGS show essentially the same chemical shifts for free and bound PBG. This is the strongest evidence that the mechanisms of these two enzymes are the same. The most exciting [sup 13]C NMR result for E. coli PBGS is the observation of additional resonances which may arise from pre-aromatic enzyme-bound intermediate(s).

OSTI ID:
6894118
Report Number(s):
CONF-9202109-; CODEN: FAJOEC
Journal Information:
FASEB Journal (Federation of American Societies for Experimental Biology); (United States), Vol. 6:1; Conference: American Society for Biochemistry and Molecular Biology and Biophysical Society joint meeting, Houston, TX (United States), 9-13 Feb 1992; ISSN 0892-6638
Country of Publication:
United States
Language:
English