This is the Wikipedia entry entitled "Cutinase". More...
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Cutinase Edit Wikipedia article
|Structure of Fusarium solani cutinase. PDB .|
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
- cutin + H2O cutin monomers
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. Plant pathogenic fungi produce extracellular degradative enzymes 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.
Cutinase is a serine esterase containing the classical Ser, His, Asp triad of serine hydrolases. 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. The protein also contains 2 disulfide bridges, which are essential for activity, their cleavage resulting in complete loss of enzymatic activity. Two cutinase-like proteins (MtCY39.35 and MtCY339.08c) have been found in the genome of the bacteria Mycobacterium tuberculosis.
- Longhi S, Czjzek M, Lamzin V, Nicolas A, Cambillau C (May 1997). "Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis". J. Mol. Biol. 268 (4): 779–99. doi:10.1006/jmbi.1997.1000. PMID 9175860.
- Ettinger WF, Thukral SK, Kolattukudy PE (1987). "Structure of cutinase gene, cDNA, and the derived amino acid sequence from phytopathogenic fungi". Biochemistry 26 (24): 7883–7892. doi:10.1021/bi00398a052.
- 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.
- Garcia-Lepe R, Nuero OM, Reyes F, Santamaria F (1997). "Lipases in autolysed cultures of filamentous fungi". Lett. Appl. Microbiol. 25 (2): 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 (13): 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 (13): 2832–40. doi:10.1021/bi00684a007. PMID 239740.
|This hydrolase article is a stub. You can help Wikipedia by expanding it.|
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Cutinase Provide feedback
No Pfam abstract.
Longhi S, Czjzek M, Lamzin V, Nicolas A, Cambillau C; , J Mol Biol 1997;268:779-799.: Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis. PUBMED:9175860 EPMC:9175860
Internal database links
|Similarity to PfamA using HHSearch:||Abhydrolase_1 VirJ PE-PPE|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000675
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 [PUBMED:]. Plant pathogenic fungi produce extracellular degradative enzymes [PUBMED:1557023] 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 [PUBMED:, PUBMED:1557023].
Cutinase is a serine esterase containing the classical Ser, His, Asp triad of serine hydrolases [PUBMED:]. 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 [PUBMED:1560844]. The protein also contains 2 disulphide bridges, which are essential for activity, their cleavage resulting in complete loss of enzymatic activity [PUBMED:]. Two cutinase-like proteins (MtCY39.35 and MtCY339.08c) have been found in the genome of the bacteria Mycobacterium tuberculosis.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||hydrolase activity (GO:0016787)|
|Biological process||metabolic process (GO:0008152)|
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Curation and family details
|Author:||Finn RD, Bateman A|
|Number in seed:||23|
|Number in full:||1537|
|Average length of the domain:||189.00 aa|
|Average identity of full alignment:||24 %|
|Average coverage of the sequence by the domain:||66.18 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||17|
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There is 1 interaction for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Cutinase domain has been found. There are 75 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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