| Entry |
|
| Name |
cutinase
|
| Class |
Hydrolases;
Acting on ester bonds;
Carboxylic-ester hydrolases
 |
| Sysname |
cutin hydrolase
|
| Reaction(IUBMB) |
cutin + H2O = cutin monomers [RN: R05793]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
|
| Comment |
Cutin, a polymeric structural component of plant cuticles, is a polymer of hydroxy fatty acids that are usually C16 or C18 and contain up to three hydroxy groups. The enzyme from several fungal sources also hydrolyses the p-nitrophenyl esters of hexadecanoic acid. It is however inactive towards several esters that are substrates for non-specific esterases.
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| Orthology |
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| Genes |
MGR: | | ANI: | | NFI: | | AFM: | | AOR: | | ANG: | | AFV: | | PCS: | | PIF: | | MTU: | | MTC: | | MRA: | | MTF: | | MTB: | | MBO: | | MBB: | | MBT: | | MPA: | | MAV: | | MSM: | | MUL: | | MVA: | | MGI: | | MSP: | | MAB: | | MMC: | | MKM: | | MJL: | | MMI: | | RHA: | | GBR: | | SRT: | | CFL: | | TCU: | | KRA: | | » show all
 |
| Reference |
|
| Authors |
Garcia-Lepe R, Nuero OM, Reyes F, Santamaria F. |
| Title |
Lipases in autolysed cultures of filamentous fungi. |
| Journal |
Lett. Appl. Microbiol. 25 (1997) 127-30. |
| Organism |
Aspergillus nidulans [GN: ani], Fusarium decemcellulare, Fusarium moniliforme, Fusarium oxysporum, Fusarium semitectum |
| Reference |
|
| Authors |
Purdy RE, Kolattukudy PE. |
| Title |
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. |
| Journal |
Biochemistry. 14 (1975) 2824-31. |
| Organism |
Fusarium solani |
| Reference |
|
| Authors |
Purdy RE, Kolattukudy PE. |
| Title |
Hydrolysis of plant cuticle by plant pathogens. Properties of cutinase I, cutinase II, and a nonspecific esterase isolated from Fusarium solani pisi. |
| Journal |
Biochemistry. 14 (1975) 2832-40. |
| Organism |
Fusarium solani |
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: CAS: 51377-41-4 |