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- *****************************
- * Matrixins cysteine switch *
- *****************************
-
- Mammalian extracellular matrix metalloproteinases (EC 3.4.24.7), also known as
- matrixins, [1] are zinc-dependent enzymes. They are secreted by cells in an
- inactive form (zymogen) that differs from the mature enzyme by the presence of
- an N-terminal propeptide. A highly conserved octapeptide is found two residues
- downstream of the C-terminal end of the propeptide. This region has been shown
- to be involved in autoinhibition of matrixins [2,3]; a cysteine within the
- octapeptide chelates the active site zinc ion, thus inhibiting the enzyme.
- This region has been called the 'cysteine switch' or 'autoinhibitor region'.
-
- A cysteine switch has been found in the following zinc proteases:
-
- - MMP-1 (EC 3.4.24.7) (interstitial collagenase).
- - MMP-2 (EC 3.4.24.24) (72 Kd gelatinase).
- - MMP-3 (EC 3.4.24.17) (stromelysin-1).
- - MMP-7 (EC 3.4.24.23) (matrilysin).
- - MMP-8 (EC 3.4.24.34) (neutrophil collagenase).
- - MMP-9 (EC 3.4.24.35) (92 Kd gelatinase).
- - MMP-10 (EC 3.4.24.22) (stromelysin-2).
- - MMP-11 (EC 3.4.24.-) (stromelysin-3).
- - Sea urchin hatching enzyme (EC 3.4.24.12) (envelysin) [4].
- - Chlamydomonas reinhardtii gamete lytic enzyme (GLE) [5].
-
- -Consensus pattern: P-R-C-[GN]-x-P-[DR]-[LIVSAP]
- [C chelates the zinc ion]
- -Sequences known to belong to this class detected by the pattern: ALL, except
- for mouse MPP-11.
- -Other sequence(s) detected in SWISS-PROT: NONE.
- -Last update: June 1994 / Text revised.
-
- [ 1] Woessner J. Jr.
- FASEB J. 5:2145-2154(1991).
- [ 2] Sanchez-Lopez R., Nicholson R., Gesnel M.C., Matrisian L.M.,
- Breathnach R.
- J. Biol. Chem. 263:11892-11899(1988).
- [ 3] Park A.J., Matrisian L.M., Kells A.F., Pearson R., Yuan Z., Navre M.
- J. Biol. Chem. 266:1584-1590(1991).
- [ 4] Lepage T., Gache C.
- EMBO J. 9:3003-3012(1990).
- [ 5] Kinoshita T., Fukuzawa H., Shimada T., Saito T., Matsuda Y.
- Proc. Natl. Acad. Sci. U.S.A. 89:4693-4697(1992).
-