F
IPR000675

Cutinase/acetylxylan esterase

InterPro entry
Short nameCutinase/axe
Overlapping
homologous
superfamilies
 
family relationships

Description

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. Cutinase is a serine esterase containing the classical Ser, His, Asp triad of serine hydrolases. The protein belongs to the α-β class, with a central β-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 disulphide bridges, which are essential for activity, their cleavage resulting in complete loss of enzymatic activity.

In the actinobacteria Kineococcus radiotolerans, this enzyme shows a C-terminal extension that is similar to the substrate binding domain of poly(hydroxybutyrate) (PHB) depolymerases
[4]
.

Acetylxylan esterase from fungi removes acetyl side groups from xylan. The catalytic core of the enzyme has an α/β/α-sandwich fold, similar to that of cutinase
[1]
.

This protein family also includes enzymes that do not show cutinase activity but exhibit esterase activity, such as phospholipases and carboxylesterases from Actinobacteria. Phospholipase Culp4 from Mycobacterium tuberculosis hydrolyses dipalmitoylphosphatidylcholine
[5, 7]
, while Carboxylesterase Culp1 from Mycobacterium tuberculosis hydrolyses various p-nitrophenol-linked aliphatic esters and has weak lipase activity
[5, 7, 6]
.

References

1.Three-dimensional structure of the catalytic core of acetylxylan esterase from Trichoderma reesei: insights into the deacetylation mechanism. Hakulinen N, Tenkanen M, Rouvinen J. J. Struct. Biol. 132, 180-90, (2000). View articlePMID: 11243887

2.Cloning and analysis of CUT1, a cutinase gene from Magnaporthe grisea. Sweigard JA, Chumley FG, Valent B. Mol. Gen. Genet. 232, 174-82, (1992). PMID: 1557023

3.Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Martinez C, De Geus P, Lauwereys M, Matthyssens G, Cambillau C. Nature 356, 615-8, (1992). View articlePMID: 1560844

4.A Novel Actinobacterial Cutinase Containing a Noncatalytic Polymer-Binding Domain. Abokitse K, Grosse S, Leisch H, Corbeil CR, Perrin-Sarazin F, Lau PCK. Appl Environ Microbiol 88, e0152221, (2022). PMID: 34705546

5.Cutinase-like proteins of Mycobacterium tuberculosis: characterization of their variable enzymatic functions and active site identification. West NP, Chow FM, Randall EJ, Wu J, Chen J, Ribeiro JM, Britton WJ. FASEB J 23, 1694-704, (2009). PMID: 19225166

6.Identification of residues involved in substrate specificity and cytotoxicity of two closely related cutinases from Mycobacterium tuberculosis. Dedieu L, Serveau-Avesque C, Canaan S. PLoS One 8, e66913, (2013). PMID: 23843969

7.Two cutinase-like proteins secreted by Mycobacterium tuberculosis show very different lipolytic activities reflecting their physiological function. Schue M, Maurin D, Dhouib R, Bakala N'Goma JC, Delorme V, Lambeau G, Carriere F, Canaan S. FASEB J 24, 1893-903, (2010). PMID: 20103719

GO terms

biological process

  • None

cellular component

  • None

Cross References

Contributing Member Database Entries
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.