Cutinase/acetylxylan esterase (IPR000675)

Short name: Cutinase/axe

Overlapping homologous superfamilies

Domain relationships



Plant pathogenic fungi produce extracellular degradative enzymes [PMID: 1557023] 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 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 [PMID: 1560844]. The protein also contains 2 disulphide bridges, which are essential for activity, their cleavage resulting in complete loss of enzymatic activity.

Acetylxylan esterase removes acetyl side groups from xylan. The catalytic core of the enzyme has an alpha/beta/alpha sandwich fold, similar to that of cutinase [PMID: 11243887].

GO terms

Biological Process

GO:0008152 metabolic process

Molecular Function

GO:0016787 hydrolase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.