76427
Penicillin Amidase from Escherichia coli
5-10 units/mg protein
Sinónimos:
Penicillin Acylase, Penicillin Amidohydrolase
Iniciar sesión para ver los precios por organización y contrato.
Seleccione un Tamaño
Acerca de este artículo
Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-753-8
MDL number:
Specific activity:
5-10 units/mg protein
Biological source:
Escherichia coli
Servicio técnico
¿Necesita ayuda? Nuestro equipo de científicos experimentados está aquí para ayudarle.
Permítanos ayudarleServicio técnico
¿Necesita ayuda? Nuestro equipo de científicos experimentados está aquí para ayudarle.
Permítanos ayudarlebiological source
Escherichia coli
form
suspension
specific activity
5-10 units/mg protein
mol wt
Mr ~70000
technique(s)
activity assay: suitable
application(s)
diagnostic assay manufacturing
storage temp.
2-8°C
Quality Level
General description
Penicillin amidase is a periplasmic 80K heterodimer with A and B chains (209 and 566 amino acids, respectively). It is widely distributed among microorganisms, including bacteria, yeast and filamentous fungi. Among all the sources, the enzyme produced by E. coli is most well-characterized and common for industrial application.
Application
Penicillin amidase was used to study its effect in release of fatty acid and HSL (homoserine lactone) from AHLs (N -acylhomoserine lactones) in degradation of antibiotics. It was used as positive control for assaying penicillin G acylase activity in the study of functional analysis of bile salt hydrolase and penicillin acylase family members in Lactobacillus sp. Penicillin amidase may be used for synthesis of 6-aminopenicillanic acid from penicillin-G and for the industrial production of β-lactam antibiotics.
Biochem/physiol Actions
The biosynthesis of Penicillin amidase in E. coli by hydrophobic protein chromatography is an inducible reaction which is regulated by metabolized carbon source (e.g. polyols, carboxylic acid etc.). It is also influenced by catabolite repression. It catalyzes the formation of amide bonds through an acyl-enzyme intermediate.
Other Notes
1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol benzylpenicillin per minute at pH 7.6 and 37°C
Characterization; In enantioselective resolution; Synthesis of ampicillin and benzylpenicillin.
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Elija entre una de las versiones más recientes:
¿Ya tiene este producto?
Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Penicillin acylase (bacterial).
T A Savidge et al.
Methods in enzymology, 43, 705-721 (1975-01-01)
V Kasche et al.
Hoppe-Seyler's Zeitschrift fur physiologische Chemie, 365(12), 1435-1443 (1984-12-01)
Hydrophobic protein chromatography was used to prepare homogeneous fractions of penicillin amidase (EC 3.5.1.11) from E. coli. The apparent ratios of the rate constants for the deacylation of the acyl-penicillin amidase formed in the hydrolysis of phenylacetylglycine or D-phenylglycine methyl
Yi-Han Lin et al.
Molecular microbiology, 47(3), 849-860 (2003-01-22)
N-acylhomoserine lactones (AHLs) are used as signal molecules by many quorum-sensing Proteobacteria. Diverse plant and animal pathogens use AHLs to regulate infection and virulence functions. These signals are subject to biological inactivation by AHL-lactonases and AHL-acylases. Previously, little was known
Lavinia Dunsmore et al.
Nature chemistry, 14(7), 754-765 (2022-06-29)
Natural products that contain ortho-quinones show great potential as anticancer agents but have been largely discarded from clinical development because their redox-cycling behaviour results in general systemic toxicity. Here we report conjugation of ortho-quinones to a carrier, which simultaneously masks
A. Guy et al.
Bioorganic & Medicinal Chemistry Letters, 3, 1041-1041 (1993)
Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.
Póngase en contacto con el Servicio técnico