Binding Affinity Determines Substrate Specificity and Enables Discovery of Substrates for N-Myristoyltransferases.

ABSTRACT: Kinetic parameters (k _cat and K _m) derived from the Michaelis-Menten equation are widely used to characterize enzymes. k _cat/K _m is considered the catalytic efficiency or substrate specificity of an enzyme toward its substrate. N-Myristoyltransferases (NMTs) catalyze the N-terminal glycine myristoylation of numerous eukaryotic proteins. Surprisingly, we find that in vitro human NMT1 can accept acetyl-CoA and catalyze acetylation with k _cat and K _m values similar to that of myristoylation. However, when both acetyl-CoA and myristoyl-CoA are present in the reaction, NMT1 catalyzes almost exclusively myristoylation. This phenomenon is caused by the dramatically different binding affinit

SUBMITTER: Su D 

PROVIDER: S-EPMC8689648 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature