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- Publisher
- Wiley
- Copyright
- International Union of Crystallography, 2012
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- DOI
- 10.1107/S1744309111053930
- pmid
- 22442220
- Publisher site
- See Article on Publisher Site
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 Å, and P41212, with unit‐cell parameters a = b = 85.6, c = 298.8 Å. 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 β‐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.
Journal
Acta Crystallographica Section F – Wiley
Published: Mar 1, 2012