PROSITE documentation PDOC00140Cutinase 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].
Two cutinase-like proteins (MtCY39.35 and MtCY339.08c) have been found in the genome of the bacteria Mycobacterium tuberculosis.
The sequence around the catalytic residues is well conserved in the sequence of the known fungal cutinases and can be used as signature patterns.
Last update:November 1997 / Patterns and text revised.
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| 1 | Authors | Ettinger W.F. Thukral S.K. Kolattukudy P.E. |
| Source | Biochemistry 26:7883-7892(1987). |
| 2 | Authors | Martinez C. De Geus P. Lauwereys M. Matthyssens G. Cambillau C. |
| Title | Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. | |
| Source | Nature 356:615-618(1992). | |
| PubMed ID | 1560844 | |
| DOI | 10.1038/356615a0 |
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