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• W1964949062 abstract "Both myeloperoxidase (MPO) and lactoperoxidase (LPO) contain high affinity bound calcium, which has been suggested to play a structural role. Asp-96 in MPO, a residue next to the histidine distal from the heme prosthetic group, has been assigned to the calcium-binding site of the enzyme by X-ray crystallography. Multiple sequence alignment of known animal peroxidases has revealed that the calcium-binding site is highly conserved. In this study, we replaced Asp-96 in MPO and the counterpart Asp-227 in LPO both with Ala by site-directed mutagenesis. The level of peroxidase activity in insect cells infected with recombinant baculoviruses and their culture supernatants was reduced to virtually zero as a result of these mutations. Immunoblotting revealed that these mutant peroxidases were expressed in the cells but not secreted as effectively as the wild-type enzymes. Our findings suggest that a functional calcium-binding site is essential for the biosynthesis of active animal peroxidases." @default.
• W1964949062 created "2016-06-24" @default.
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• W1964949062 date "2001-03-01" @default.
• W1964949062 modified "2023-10-16" @default.
• W1964949062 title "Mutations Affecting the Calcium-Binding Site of Myeloperoxidase and Lactoperoxidase" @default.
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• W1964949062 doi "https://doi.org/10.1006/bbrc.2001.4448" @default.
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