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Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from Alcaligenes faecalis
- 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 thatThe 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.…
Verfasserangaben: | Nishant Kumar Varshney, R. Suresh Kumar, Zoya Ignatova, Asmita Prabhune, Archana Pundle, Eleanor Dodson, C. G. Suresh |
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DOI: | https://doi.org/10.1107/S1744309111053930 |
ISSN: | 1744-3091 |
Titel des übergeordneten Werks (Englisch): | Acta crystallographica : Section F, Structural biology communications |
Verlag: | Wiley-Blackwell |
Verlagsort: | Malden |
Publikationstyp: | Wissenschaftlicher Artikel |
Sprache: | Englisch |
Jahr der Erstveröffentlichung: | 2012 |
Erscheinungsjahr: | 2012 |
Datum der Freischaltung: | 26.03.2017 |
Freies Schlagwort / Tag: | Ntn hydrolases; calcium binding; disulfide bridges; orthorhombic form; tetragonal form; thermostability |
Band: | 68 |
Ausgabe: | 3 |
Seitenanzahl: | 5 |
Erste Seite: | 273 |
Letzte Seite: | 277 |
Fördernde Institution: | Council for Scientific and Industrial Research (CSIR), New Delhi |
Organisationseinheiten: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie |
Peer Review: | Referiert |