@article{VarshneyKumarIgnatovaetal.2012,
  author    = {Varshney, Nishant Kumar and Kumar, R. Suresh and Ignatova, Zoya and Prabhune, Asmita and Pundle, Archana and Dodson, Eleanor and Suresh, C. G.},
  title     = {Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from Alcaligenes faecalis},
  series = {Acta crystallographica : Section F, Structural biology communications},
  volume    = {68},
  journal   = {Acta crystallographica : Section F, Structural biology communications},
  number    = {3},
  publisher = {Wiley-Blackwell},
  address   = {Malden},
  issn      = {1744-3091},
  doi       = {10.1107/S1744309111053930},
  pages     = {273 -- 277},
  year      = {2012},
  abstract  = {The enzyme penicillin G acylase (EC 3.5.1.11) catalyzes amide-bond cleavage in benzylpenicillin (penicillin G) to yield 6-aminopenicillanic acid, an intermediate chemical used in the production of semisynthetic penicillins. A thermostable penicillin G acylase from Alcaligenes faecalis (AfPGA) has been crystallized using the hanging-drop vapour-diffusion method in two different space groups: C2221, with unit-cell parameters a = 72.9, b = 86.0, c = 260.2 angstrom, and P41212, with unit-cell parameters a = b = 85.6, c = 298.8 angstrom. Data were collected at 293 K and the structure was determined using the molecular-replacement method. Like other penicillin acylases, AfPGA belongs to the N-terminal nucleophilic hydrolase superfamily, has undergone post-translational processing and has a serine as the N-terminal residue of the beta-chain. A disulfide bridge has been identified in the structure that was not found in the other two known penicillin G acylase structures. The presence of the disulfide bridge is perceived to be one factor that confers higher stability to this enzyme.},
  language  = {en}
}