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J Biol Chem, Vol. 274, Issue 3, 1193-1195, January 15, 1999
From the Department of Biochemistry, Brandeis University,
Waltham, Massachusetts 02453-2728
Two enzymes, designated, E-2 and E-2', catalyze
different oxidation reactions of an aci-reductone intermediate in the
methionine salvage pathway. E-2 and E-2', overproduced in
Escherichia coli from the same gene, have the same protein
component. E-2 and E-2' are separable on an anion exchange column or a
hydrophobic column. Their distinct catalytic and chromatographic
properties result from binding different metals. The apo-enzyme,
obtained after metal is removed from either enzyme, is catalytically
inactive. Addition of Ni2+ or Co2+ to the
apo-protein yields E-2 activity. E-2' activity is obtained when
Fe2+ is added. Production in intact E. coli of
E-2 and E-2' depends on the availability of the corresponding metals.
These observations suggest that the metal component dictates reaction specificity.
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