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Photoaffinity labeling with the activator IMP and site-directed mutagenesis of histidine 995 of carbamoyl phosphate synthetase from Escherichia coli demonstrate that the binding site for IMP overlaps with that for the inhibitor UMP.
Bueso J, Cervera J, Fresquet V, Marina A, Lusty CJ, Rubio V. Bueso J, et al. Among authors: cervera j. Biochemistry. 1999 Mar 30;38(13):3910-7. doi: 10.1021/bi982871f. Biochemistry. 1999. PMID: 10194302
However, the mutation selectively induced changes in the activation by IMP and the inhibition by UMP, and it abolished the photolabeling of the enzyme by IMP without affecting the photolabeling by the inhibitor UMP. Since UMP is cross-linked to Lys993 [Cervera, J., …
However, the mutation selectively induced changes in the activation by IMP and the inhibition by UMP, and it abolished the photolabeling of …
362 results