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Citation: Z. Ignatova et al., Role of the intracellular proteolysis in the production of the periplasmicpenicillin amidase in Escherichia coli, BIOTECH LET, 22(21), 2000, pp. 1727-1732
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Citation: Z. Ignatova et al., The relative importance of intracellular proteolysis and transport on the yield of the periplasmic enzyme penicillin amidase in Escherichia coli, ENZYME MICR, 26(2-4), 2000, pp. 165-170
Citation: B. Galunsky et al., Comparative study of substrate- and stereospecificity of penicillin G amidases from different sources and hybrid isoenzymes, MONATS CHEM, 131(6), 2000, pp. 623-632
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Citation: L. Hewitt et al., Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft, J MOL BIOL, 302(4), 2000, pp. 887-898
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Citation: V. Kasche et al., Intramolecular autoproteolysis initiates the maturation of penicillin amidase from Escherichia coli, BBA-PROT ST, 1433(1-2), 1999, pp. 76-86
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Citation: A. Spiess et al., pH gradients in immobilized amidases and their influence on rates and yields of beta-lactam hydrolysis, BIOTECH BIO, 62(3), 1999, pp. 267-277
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Citation: Z. Ignatova et al., Proteolytic processing of penicillin amidase from Alcaligenes faecalis cloned in E-coli yields several active forms, BIOTECH LET, 20(10), 1998, pp. 977-982