Escherichia coli methionine aminopeptidase with Tyr168 to alanine substitution can improve the N-terminal processing of recombinant proteins with valine at the penultimate position.
Liu
Li-Fan
LF
Institute of Molecular Biology, Academia Sinica, NanKang Taipei 11529, Taiwan, ROC.
Hsieh
Cheng-Hsilin
CH
Liu
Pei-Fen
PF
Tsai
Shu-Ping
SP
Tam
Ming F
MF
D000409:Alanine / Q000235:genetics / Q000378:metabolism*; D000626:Aminopeptidases / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular / Q000379:methods; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D063208:Methionyl Aminopeptidases; D011499:Protein Processing, Post-Translational / Q000502:physiology; D013379:Substrate Specificity; D014443:Tyrosine / Q000235:genetics / Q000378:metabolism*; D014633:Valine / Q000378:metabolism*
D014443:Tyrosine; D000626:Aminopeptidases; D063208:Methionyl Aminopeptidases; D014633:Valine; D000409:Alanine