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Table 2 Relative sequence specificities of matrixins influenced by the P1' position

From: Engineering of tissue inhibitor of metalloproteinases mutants as potential therapeutics

  Relative rate of hydrolysis
P4–P3–P2–P1 ~ P1'-P2'-P3'-P4' MMP-1 MMP-2 MMP-3
Gly-Pro-Gln-Gly ~ Ile-Ala-Gly-Gln 100 100 100
Gly-Pro-Gln-Gly ~ Leu-Ala-Gly-Gln 130 88 110
Gly-Pro-Gln-Gly ~ Val-Ala-Gly-Gln 9.1 30 53
Gly-Pro-Gln-Gly ~ Ser-Ala-Gly-Gln 5.9 15 45
Gly-Pro-Gln-Gly ~ Phe-Ala-Gly-Gln 20 55 140
Gly-Pro-Gln-Gly ~ Met-Ala-Gly-Gln 110 230 60
Gly-Pro-Gln-Gly ~ Gln-Ala-Gly-Gln 28 34 38
Gly-Pro-Gln-Gly ~ Glu-Ala-Gly-Gln <0.5 <0.5 <0.002
Gly-Pro-Gln-Gly ~ Arg-Ala-Gly-Gln <0.5 <0.5 <4.9
  1. MMP, matrix metalloproteinase.