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- W2004385217 abstract "Phosphoenolpyruvate carboxylase (EC 4.1.1.31, PEPC) from maize leaves contains about thirty two half-cystine residues in the protein molecule. Eight thiol groups are free accessible groups. Next four thiol groups are free groups determined when the enzyme is denatured by sodium dodecylsulfate -only. Next four thiol groups are available only after the treatment with dithiothreitol. Sixteen halfcystine residues are firmly bound in the enzyme protein molele. PEPC exposed to dithiothreitol or 2- mere aptoethanol exhibits an increase in the enzymic activity. The enzyme is modified by p-chloromercuribenzoate and CU2+ ions and these modifications result in inactivation of the enzyme. The effects of the sulfhydryl modifiers on the changes of the tetrameric structure of the enzyme are examined." @default.
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- W2004385217 date "1988-01-01" @default.
- W2004385217 modified "2023-09-23" @default.
- W2004385217 title "The Role of Cysteine and Cystine Residues in Phosphoenolpyruvate Carboxylase from Maize Leaves" @default.
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- W2004385217 doi "https://doi.org/10.1016/s0015-3796(88)80062-3" @default.
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