Crystallization and X-ray structure analysis of a thermostable penicillin G acylase fromAlcaligenes faecalis
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چکیده
منابع مشابه
Molecular cloning and analysis of the gene encoding the thermostable penicillin G acylase from Alcaligenes faecalis.
Alcaligenes faecalis penicillin G acylase is more stable than the Escherichia coli enzyme. The activity of the A. faecalis enzyme was not affected by incubation at 50 degrees C for 20 min, whereas more than 50% of the E. coli enzyme was irreversibly inactivated by the same treatment. To study the molecular basis of this higher stability, the A. faecalis enzyme was isolated and its gene was clon...
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Kluyvera citrophila penicillin G acylase (KcPGA) has recently attracted increased attention relative to the well studied and commonly used Escherichia coli PGA (EcPGA) because KcPGA is more resilient to harsh conditions and is easier to immobilize for the industrial hydrolysis of natural penicillins to generate the 6-aminopenicillin (6-APA) nucleus, which is the starting material for semi-synth...
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The PGA enzyme belongs to the family of N-terminal nucleophile (Ntn) hydrolases. The enzyme Penicillin G Acylase (PGA) mainly produced from Penicillium chrysogenum, E.coli. The synthesis of PGA enzyme is depends on the physico-chemical parameters like carbon source, pH, temperature and media were optimized for higher production of enzyme. There are different methods of purification of PGA enzym...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section F Structural Biology and Crystallization Communications
سال: 2012
ISSN: 1744-3091
DOI: 10.1107/s1744309111053930