Abstract
Penicillin G amidase (PGA, EC 3.5.1.11) from E. coli is a hydrolytic enzyme belonging to the structural superfamily termed N-terminal nucleophile (Ntm) amidohydrolase. It consists of two different subunits-alpha subunit (109 aa, 24 kDa) and beta subunit (557 aa, 62 kDa)-which are held together by non covalent forces. It does not contain any cystein or disulfide bridges. The N-terminal serine residue (Ser290) of the beta subunit constitutes the base in the catalytic cycle and acts as a nucleophile, whereas the alpha subunit mediates the substrate specificity. PGA displays a compact cone-shaped form with a single Cat2+ binding site. Cat2+-binding is presumed to be an important trigger of processing [1].
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Bochtler-Hock, H., Wedekind, F. (2003). Cell-Free Expression of the Heterodimeric Protein Penicillin G Amidase in a Functionally Active Form. In: Swartz, J.R. (eds) Cell-Free Protein Expression. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-59337-6_22
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DOI: https://doi.org/10.1007/978-3-642-59337-6_22
Publisher Name: Springer, Berlin, Heidelberg
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