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. Author manuscript; available in PMC: 2009 Aug 1.
Published in final edited form as: Biol Chem. 2008 Aug;389(8):1107–1115. doi: 10.1515/BC.2008.122

Figure 6. Mutation of non-catalytic residues lining the GlpG active site hinder protease activity.

Figure 6

A. Top view of GlpG (PDB N2RF), with the L1 loop down. Side-chains of conserved non-catalytic active sites residues under investigation are highlighted in black. B and C. Western analysis of cultures expressing either wildtype of mutant GlpG proteases with the Spitz substrate. All mutant enzymes show a decrease in substrate processing (cleavage product denoted by black arrow). UN and SA denote uninduced wildtype and S201A-expressing cultures, respectively. Location of protein mass standards (in kDa) are depicted on the left.