Targeted and proximity-dependent promiscuous protein biotinylation by a mutant Escherichia coli biotin protein ligase

A method for general protein biotinylation by enzymatic means has been developed. A mutant form (R118G) of the biotin protein ligase (BirA) of Escherichia coli is used and biotinylation is thought to proceed by chemical acylation of protein lysine side chains by biotinoyl-5′-AMP released from the mu...

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Veröffentlicht in:	The Journal of nutritional biochemistry 2005-07, Vol.16 (7), p.416-418
1. Verfasser:	Cronan, John E.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Monophosphate - analogs & derivatives Adenosine Monophosphate - chemistry Adenosine Monophosphate - metabolism aminoacylation bacterial proteins binding proteins biotin Biotin - analogs & derivatives Biotin - chemistry Biotin - metabolism Carbon-Nitrogen Ligases - genetics Carbon-Nitrogen Ligases - metabolism cell physiology Chloramphenicol O-Acetyltransferase - chemistry Chloramphenicol O-Acetyltransferase - metabolism enzymatic hydrolysis Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Immunoglobulins - chemistry Immunoglobulins - metabolism ligases Lysine - metabolism mutants Mutation Protein Engineering - methods protein-protein interactions Repressor Proteins - genetics Repressor Proteins - metabolism Ribonuclease, Pancreatic - chemistry Ribonuclease, Pancreatic - metabolism Serum Albumin, Bovine - chemistry Serum Albumin, Bovine - metabolism Transcription Factors - genetics Transcription Factors - metabolism
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