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- W2073945170 abstract "1. Fully active δ-aminolevulinate dehydratase which contained 1 zinc atom and 8 sulfhydryl groups/subunit was purified from bovine liver. 2. Two cysteine residues, two histidine residues and one zinc atom were shown to constitute the active site. 3. At least one free sulfhydryl group is essential for activation of δ-aminolevulinate, supposedly its intactness being protected by coordination of the adjacent SH group with the zinc ion. This zinc was also suggested to be further coordinated with one of the histidine residues. 4. Lead replaced stoichiometrically the zinc yielding the inactivated enzyme. 5. A model for the active site and a reaction scheme were proposed." @default.
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- W2073945170 date "1980-01-01" @default.
- W2073945170 modified "2023-09-23" @default.
- W2073945170 title "Zinc and cysteine residues in the active site of bovine liver 5-aminolevulinic acid dehydratase" @default.
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- W2073945170 doi "https://doi.org/10.1016/0020-711x(80)90157-3" @default.
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