| Autor: |
Piotraschke, Elke, Nurk, Allan, Galunsky, Boris, Kasche, Volker |
| Zdroj: |
Biotechnology Letters; February 1994, Vol. 16 Issue: 2 p119-124, 6p |
| Abstrakt: |
A cross-species penicillin G amidase (PGA) gene (pac) coding for an α-peptide and a linker peptide fromK. citrophilaATCC 21285 and a β-peptide fromE. coliATCC 11105 has been constructed and cloned inE. coli. The naturally occurring PGA specific processing pathway led to the formation of a hybrid enzyme which was catalytically active. In comparison with the two wild-type enzymes the hybrid PGA was found to have higherkcatvalues for the three tested substrates benzylpenicillin, ampicillin and 6-nitro-3-phenylacetamido-benzoic acid (NIPAB).Kmwas between the values of the wild-type enzymes or close to that ofK. citrophila. The presented method for protein design of processed enzymes, like PGA, can be applied to combine enzyme properties from different species for special applications. |
| Databáze: |
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