Ontology highlight
ABSTRACT:
SUBMITTER: Zheng Y
PROVIDER: S-EPMC1112042 | biostudies-literature | 2005 Jun
REPOSITORIES: biostudies-literature
Zheng Yu Y Roberts Richard J RJ Kasif Simon S Guan Chudi C
Journal of bacteriology 20050601 11
Two genes in the Escherichia coli genome, ypdE and ypdF, have been cloned and expressed, and their products have been purified. YpdF is shown to be a metalloenzyme with Xaa-Pro aminopeptidase activity and limited methionine aminopeptidase activity. Genes homologous to ypdF are widely distributed in bacterial species. The unique feature in the sequences of the products of these genes is a conserved C-terminal domain and a variable N-terminal domain. Full or partial deletion of the N terminus in Y ...[more]