Cutinase

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Cutinase
Identifiers
Symbol	Cutinase
Pfam	PF01083
InterPro	IPR000675
PROSITE	PDOC00140
SCOP	1cex
OPM family	135
OPM protein	1oxm
Available PDB structures: 2axe :28-234 1g66A:28-234 1bs9 :28-234 1qozB:32-238 1cua :45-224 1cub :45-224 1xzm :45-224 1cuy :45-224 1cuwA:45-224 1cudB:45-224 1xzj :45-224 1cug :45-224 1xzb :45-224 1ffb :45-224 1ffa :45-224 1oxmB:45-224 1cue :45-224 1cuh :45-224 1cuv :45-224 1cus :45-224 1xzkA:45-224 1agy :45-224 1ffd :45-224 1cuf :45-224 1xze :45-224 1xzd :45-224 1cuu :45-224 1cui :45-224 1xzc :45-224 1xzh :45-224 2cut :45-224 1cuz :45-224 1xzl :45-224 1cex :45-224 1cuc :45-224 1xzg :45-224 1xzi :45-224 1ffc :45-224 1ffe :45-224 1xzf :45-224 1cux :45-224 1xza :45-224 1cuj :45-224

A cutinase (EC 3.1.1.74) is an enzyme that catalyzes the chemical reaction

cutin + H₂O $\rightleftharpoons$ cutin monomers

Thus, the two substrates of this enzyme are cutin and H₂O, whereas its product is cutin monomer.

This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is cutin hydrolase.

Aerial plant organs are protected by a cuticle composed of an insoluble polymeric structural compound, cutin, which is a polyester composed of hydroxy and hydroxyepoxy fatty acids^[1]. Plant pathogenic fungi produce extracellular degradative enzymes^[2] that play an important role in pathogenesis. They include cutinase, which hydrolyses cutin, facilitating fungus penetration through the cuticle. Inhibition of the enzyme can prevent fungal infection through intact cuticles. Cutin monomers released from the cuticle by small amounts of cutinase on fungal spore surfaces can greatly increase the amount of cutinase secreted by the spore, the mechanism for which process is as yet unknown^[1]^[2].

Cutinase is a serine esterase containing the classical Ser, His, Asp triad of serine hydrolases^[1]. The protein belongs to the alpha-beta class, with a central beta-sheet of 5 parallel strands covered by 5 helices on either side of the sheet. The active site cleft is partly covered by 2 thin bridges formed by amino acid side chains, by contrast with the hydrophobic lid possessed by other lipases^[3]. The protein also contains 2 disulfide bridges, which are essential for activity, their cleavage resulting in complete loss of enzymatic activity^[1]. Two cutinase-like proteins (MtCY39.35 and MtCY339.08c) have been found in the genome of the bacteria Mycobacterium tuberculosis.

[edit] References

^ ^a ^b ^c ^d Ettinger WF, Thukral SK, Kolattukudy PE (1987). "Structure of cutinase gene, cDNA, and the derived amino acid sequence from phytopathogenic fungi". Biochemistry 26: 7883–7892. doi:10.1021/bi00398a052.
^ ^a ^b Sweigard JA, Chumley FG, Valent B (1992). "Cloning and analysis of CUT1, a cutinase gene from Magnaporthe grisea". Mol. Gen. Genet. 232 (2): 174–182. PMID 1557023.
^ Cambillau C, Martinez C, De Geus P, Lauwereys M, Matthyssens G (1992). "Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent". Nature 356 (6370): 615–618. doi:10.1038/356615a0. PMID 1560844.

IUBMB entry for 3.1.1.74
BRENDA references for 3.1.1.74 (Recommended.)
PubMed references for 3.1.1.74
PubMed Central references for 3.1.1.74
Google Scholar references for 3.1.1.74
Garcia-Lepe R, Nuero OM, Reyes F, Santamaria F (1997). "Lipases in autolysed cultures of filamentous fungi". Lett. Appl. Microbiol. 25: 127–30. doi:10.1046/j.1472-765X.1997.00187.x. PMID 9281862.
Purdy RE, Kolattukudy PE (1975). "Hydrolysis of plant cuticle by plant pathogens. Purification, amino acid composition, and molecular weight of two isozymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi". Biochemistry. 14: 2824–31. doi:10.1021/bi00684a006. PMID 1156575.
Purdy RE, Kolattukudy PE (1975). "Hydrolysis of plant cuticle by plant pathogens. Properties of cutinase I, cutinase II, and a nonspecific esterase isolated from Fusarium solani pisi". Biochemistry. 14: 2832–40. doi:10.1021/bi00684a007. PMID 239740.