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- ************************************
- * Cutinase active sites signatures *
- ************************************
-
- Cutinase [1] is an extracellular fungal enzyme that catalyzes the hydrolysis
- of cutin, an insoluble lipid-polyester that forms the structure of plant
- cuticle. Cutinase allows pathogenic fungi to penetrate through the host plant
- cuticular barrier during the initial stage of fungal infection. Cutinase is a
- serine esterase which contains the classical catalytic triad (Asp, Ser, and
- His) found in the serine hydrolases [2].
-
- The sequence around the catalytic residues is well conserved in the sequence
- of the known fungal cutinases and can be used as signature patterns.
-
- -Consensus pattern: G-G-Y-S-Q-G
- [S is an active site residue]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Consensus pattern: D-x-V-C-x-G-[ST]-[LIVMF](3)-x(3)-H
- [D and H are active site residues]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Last update: October 1993 / Patterns and text revised.
-
- [ 1] Ettinger W.F., Thukral S.K., Kolattukudy P.E.
- Biochemistry 26:7883-7892(1987).
- [ 2] Martinez C., De Geus P., Lauwereys M., Matthyssens G., Cambillau C.
- Nature 356:615-618(1992).
-