title: [Activity of the SrfAC-A domain from Bacillus subtilis fmbj].
abstract: OBJECTIVE
  We studied the A domain of surfactin synthase in vitro to obtain new surfactin analogues.
  
  
  METHODS
  We cloned the srfAC-A gene from Bacillus subtilis fmbj by PCR, and constructed a recombinant expression vector named pET-23a-srfAC-A. Furthermore, the SrfAC-A domain was expressed in E. coli BL21 (DE3) and purified by Ni-NTA agarose column. Then the activity of srfAC-A domain was detected.
  
  
  RESULTS
  The srfAC-A domain had specificity towards Ile, but almost no activity to other amino acids.
  
  
  CONCLUSIONS
  The independent A domain from surfactin synthase had selectivity to specific amino acids in vitro.
authors: College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China. hzdaxia@126.com
authors: Lixia
authors: L
authors: Liu
authors: Zhaoxin
authors: Z
authors: Lu
authors: Fengxia
authors: F
authors: Lv
authors: Chong
authors: C
authors: Zhang
authors: Xiaomei
authors: X
authors: Bie
mesh_terms: D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D003001:Cloning, Molecular; D004789:Enzyme Activation; D015870:Gene Expression; D008969:Molecular Sequence Data; D010453:Peptide Synthases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D054730:Protein Interaction Domains and Motifs; D011994:Recombinant Proteins; D016415:Sequence Alignment; D012995:Solubility
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins; D010453:Peptide Synthases; C069542:surfactin synthetase