Characterization of full length and truncated type I human methionine aminopeptidases expressed from Escherichia coli.

@article{Li2004CharacterizationOF,
  title={Characterization of full length and truncated type I human methionine aminopeptidases expressed from Escherichia coli.},
  author={Jingya Li and Ling-Ling Chen and Y Cui and Qun-li Luo and Min Gu and Fa-jun Nan and Qi-zhuang Ye},
  journal={Biochemistry},
  year={2004},
  volume={43 24},
  pages={7892-8}
}
Methionine aminopeptidase (MetAP) carries out an essential posttranslational modification of nascent proteins by removing the initiator methionine and is recognized as a potential target for developing antibacterial, antifungal, and anticancer agents. We have established an Escherichia coli expression system for human type I MetAP (HsMetAP1) and characterized the full length HsMetAP1 and its N-terminal-truncated mutants HsMetAP1(Delta1-66) and HsMetAP1(Delta1-135) for hydrolysis of several… CONTINUE READING