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. Author manuscript; available in PMC: 2008 Sep 16.
Published in final edited form as: Biochemistry. 2006 Mar 28;45(12):3863–3874. doi: 10.1021/bi052252o

Figure 4.

Figure 4

Cleavage site specificity of MMP-20. The graphs on the right show the relative distribution of amino acid residues at positions C-terminal (P1′-P4′) to the MMP-20 cleavage site. These sites were identified by sequencing an N-terminally acetylated random peptide dodecamer (Ac-XXXXXXXXXXXX). Data were normalized so that a value of 1 corresponded to the average quantity per amino acid in a given sequencing cycle and would indicate no selectivity. Tryptophan was not included in the analysis because of poor yield during sequencing. The figures on the left represent the positions amino terminal to the MMP-20 cleavage site. For the P3 position data shown were generated using the library MAXXXXXLRGAARE(K-biotin). For all other positions the P3 proline library MGXXPXXLRGGGEE(K-biotin) was used. Glutamine and threonine were omitted in some cycles because of high background on the sequencer. Data were normalized as for the primed sites.