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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.