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- W2023602222 abstract "The region of Escherichia coli adenylyl cyclase spanned by glycine-55 to threonine-65 was tested for its importance for enzyme activity. Site-directed mutagenesis was used to replace glycine-55 and glycine-60 as well as lysine-59, leucine-63 and threonine-65 with other amino acids. While substitution of glycine-55 with aspartic acid produced no significant change in kinetic parameters, the change of glycine-60 to aspartic acid or asparagine eliminated binding to 8-azido-ATP and decreased the Vmax (two orders of magnitude) and Km (factor of four-five). Smaller effects on kinetic parameters were observed with substitutions of lysine-59, leucine-63 or threonine-65." @default.
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- W2023602222 date "1992-02-01" @default.
- W2023602222 modified "2023-09-24" @default.
- W2023602222 title "Requirement for gly-60 of Escherichia coli adenylyl cyclase for ATP binding and catalytic activity" @default.
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- W2023602222 doi "https://doi.org/10.1016/0006-291x(92)91861-j" @default.
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