{PDOC00140}
{PS00155; CUTINASE_1}
{PS00931; CUTINASE_2}
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* Cutinase active sites signatures *
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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.

-Consensus pattern: P-x-[STA]-x-[LIV]-[IVT]-x-[GS]-G-Y-S-[QL]-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: C-x(3)-D-x-[IV]-C-x-G-[GST]-x(2)-[LIVM]-x(2,3)-H
                    [D and H are active site residues]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for MtCY339.08c.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: November 1997 / 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.
     "Fusarium solani cutinase is a lipolytic enzyme with a catalytic
     serine accessible to solvent."
     Nature 356:615-618(1992).
     PubMed=1560844; DOI=10.1038/356615a0

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