P3319
Penicillin Amidase from Escherichia coli
ammonium sulfate suspension, ≥10 units/mg protein (E1%/280)
Synonym(s):
Penicillin Acylase, Penicillin Amidohydrolase
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About This Item
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biological source
Escherichia coli
Quality Level
form
ammonium sulfate suspension
specific activity
≥10 units/mg protein (E1%/280)
shipped in
wet ice
Storage temp.
2-8°C
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Unit Definition
One unit will hydrolyze 1.0 μmole of benzylpenicillin per min at pH 7.8 at 37°C.
Physical form
Suspension in 0.1 M phosphate, pH 7.5 and 3 M ammonium sulfate
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Veronese, F., et al.
Il Farmaco Ed. Sc., 36, 663-663 (1981)
Nishant Kumar Varshney et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 68(Pt 3), 273-277 (2012-03-24)
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
Özlem Akkaya et al.
World journal of microbiology & biotechnology, 28(5), 2159-2164 (2012-07-19)
Penicillin G acylase (PA) is an important enzyme used in the industrial production of b-lactam antibiotics. In this study, the effects of mutations in the translation initiation region of the Escherichia coli pac gene, encoding periplasmic PA, were examined. Several
Pedro Valencia et al.
New biotechnology, 29(2), 218-226 (2011-09-20)
A mathematical model is presented for the kinetically controlled synthesis of cephalexin that describes the heterogeneous reaction-diffusion process involved in a batch reactor with glyoxyl-agarose immobilized penicillin acylase. The model is based on equations considering reaction and diffusion components. Reaction
Jun Yin et al.
The Journal of biological chemistry, 286(27), 24476-24486 (2011-05-18)
Cephalosporin acylase (CA) precursor is translated as a single polypeptide chain and folds into a self-activating pre-protein. Activation requires two peptide bond cleavages that excise an internal spacer to form the mature αβ heterodimer. Using Q-TOF LC-MS, we located the
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