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. Author manuscript; available in PMC: 2014 Jun 3.
Published in final edited form as: Nat Struct Mol Biol. 2009 Sep 20;16(10):1101–1108. doi: 10.1038/nsmb.1668

Figure 6.

Figure 6

Biochemical and kinetic analysis of cleavage-sites identified by N-terminomics. Many E. coli proteins that were identified as substrates of human caspase-3, and containing only 1 cleavage-site were recombinantly expressed, purified, and subjected to in vitro cleavage by human caspase-3. The cleavage-site P4-P1’ amino acids are colored black with the P1 residue in stick format. Substrate cleavage-sites were identified by N-terminal sequencing of the proteolytic fragments using Edman degradation. The E1/2 values were measured based on the disappearance of the full-length substrate using densitometry. These values were used to calculate kcat/KM for each substrate.