Cutinase
From Proteopedia
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| - | <StructureSection load='4oyl' size='350' side='right' caption='Structure of cutinase complex with inhibitor E600 (PDB entry [[4oyl]])' scene=''> | + | <StructureSection load='4oyl' size='350' side='right' caption='Structure of cutinase complex with inhibitor E600 (PDB entry [[4oyl]])' scene='55/551226/Cv/1'> |
'''Cutinase''' (CUT) catalyzes the conversion of cutin to cutin monomers. Cutin is a main component of the plant cuticle. Polymeric cutin which is composed of hydroxyl and hydroxyepoxy fatty acids is found in the outer layer of plants. CUT is found in fungi and bacteria. CUT degrades the cutin enabling pathogens’ penetration into plant cells. CUT is inhibited by organophosphates like E600 (diethyl-p-nitrophenyl phosphate) and organophosphonates.<ref>PMID:9175860</ref> | '''Cutinase''' (CUT) catalyzes the conversion of cutin to cutin monomers. Cutin is a main component of the plant cuticle. Polymeric cutin which is composed of hydroxyl and hydroxyepoxy fatty acids is found in the outer layer of plants. CUT is found in fungi and bacteria. CUT degrades the cutin enabling pathogens’ penetration into plant cells. CUT is inhibited by organophosphates like E600 (diethyl-p-nitrophenyl phosphate) and organophosphonates.<ref>PMID:9175860</ref> | ||
Revision as of 11:47, 21 December 2015
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3D Structures of cutinase
Updated on 21-December-2015
References
- ↑ Longhi S, Czjzek M, Lamzin V, Nicolas A, Cambillau C. Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis. J Mol Biol. 1997 May 16;268(4):779-99. PMID:9175860 doi:http://dx.doi.org/10.1006/jmbi.1997.1000
- ↑ Kold D, Dauter Z, Laustsen AK, Brzozowski AM, Turkenburg JP, Nielsen AD, Koldso H, Petersen E, Schiott B, De Maria L, Wilson KS, Svendsen A, Wimmer R. Thermodynamic and structural investigation of the specific SDS binding of humicola insolens cutinase. Protein Sci. 2014 May 16. doi: 10.1002/pro.2489. PMID:24832484 doi:http://dx.doi.org/10.1002/pro.2489
