Ontology highlight
ABSTRACT:
SUBMITTER: Liao YD
PROVIDER: S-EPMC2279930 | biostudies-literature | 2004 Jul
REPOSITORIES: biostudies-literature
Liao You-Di YD Jeng Jen-Chong JC Wang Chiu-Feng CF Wang Sui-Chi SC Chang Shu-Ting ST
Protein science : a publication of the Protein Society 20040701 7
The removal of N-terminal translation initiator Met by methionine aminopeptidase (MetAP) is often crucial for the function and stability of proteins. On the basis of crystal structure and sequence alignment of MetAPs, we have engineered Escherichia coli MetAP by the mutation of three residues, Y168G, M206T, Q233G, in the substrate-binding pocket. Our engineered MetAPs are able to remove the Met from bulky or acidic penultimate residues, such as Met, His, Asp, Asn, Glu, Gln, Leu, Ile, Tyr, and Tr ...[more]