PROSITE documentation PDOC00140 [for PROSITE entry PS00155]

Cutinase active sites signatures





Description

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.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

CUTINASE_1, PS00155; Cutinase, serine active site  (PATTERN)

CUTINASE_2, PS00931; Cutinase, aspartate and histidine active sites  (PATTERN)


References

1AuthorsEttinger W.F., Thukral S.K., Kolattukudy P.E.
SourceBiochemistry 26:7883-7892(1987).

2AuthorsMartinez C., De Geus P., Lauwereys M., Matthyssens G., Cambillau C.
TitleFusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent.
SourceNature 356:615-618(1992).
PubMed ID1560844
DOI10.1038/356615a0



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