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Article

Improved A. faecalis penicillin amidase mutant retains the thermodynamic and pH stability of the wild type enzyme.

The protein journal - 1 Apr 2010

Yuryev Ruslan, Kasche Volker, Ignatova Zoya, Galunsky Boris

Abstract excerpt

Penicillin amidase from Alacaligenes faecalis is an attractive biocatalyst for hydrolysis of penicillin G for production of 6-aminopenicillanic acid, which is used in the synthesis of semi-synthetic beta-lactam antibiotics. Recently a mutant of this enzyme with extended C-terminus of the A-chain comprising parts of the connecting linker peptide was constructed. Its turnover number for the hydrolysis of penicillin...

Topics

Alcaligenes faecalis
Anilino Naphthalenesulfonates
Bacterial Proteins
Escherichia coli
Hydrogen-Ion Concentration
Kinetics
Mutation
Penicillin Amidase
Protein Folding
Protein Stability
Recombinant Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Structural Homology, Protein

Temperature

Thermodynamics

Urea

Source

Identifiers

PMID: 20224955
DOI: 10.1007/s10930-010-9238-4

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