Cutinase
Cutinase | ||
---|---|---|
![]() |
||
according to PDB 1CEX | ||
Mass / length primary structure | 230 amino acids | |
Identifier | ||
External IDs | ||
Enzyme classification | ||
EC, category | 3.1.1.74 , carboxyl ester hydrolase | |
Substrate | Cutin + H 2 O | |
Products | Cutin monomers |
Cutinase or cutin hydrolase is an enzyme that belongs to the α / β hydrolases and hydrolyses cutin .
properties
Cutinase is produced by some phytopathogenic fungi and bacteria , among others . Through the cutinase, the fungi are able to break down the ester bond of the cutin in the cuticula of the plants and thus penetrate the plants.
Like all enzymes , however , they catalyze both forward and reverse reactions , which means that under suitable conditions they are able to synthesize polyesters by polycondensation .
literature
- S. Longhi, C. Cambillau: Structure-activity of cutinase, a small lipolytic enzyme. In: Biochimica et Biophysica Acta . Volume 1441, Numbers 2-3, November 1999, pp 185-196, PMID 10570246 .
Individual evidence
- ↑ JA Sweigard, FG Chumley, B. Valent: Cloning and analysis of CUT1, a cutinase gene from Magnaporthe grisea. In: Molecular & general genetics: MGG. Volume 232, Number 2, March 1992, pp. 174-182, PMID 1557023 .
- ↑ S. Chen, L. Su, J. Chen, J. Wu: Cutinase: characteristics, preparation, and application. In: Biotechnology Advances . Volume 31, number 8, December 2013, pp. 1754-1767, doi : 10.1016 / j.biotechadv.2013.09.005 . PMID 24055682 .
- ↑ PE Kolattukudy: polyester in higher plants. In: Advances in Biochemical Engineering / Biotechnology . Volume 71, 2001, pp. 1-49, PMID 11217409 .
- ^ TF Pio, GA Macedo: Cutinases: properties and industrial applications. In: Advances in applied microbiology. Volume 66, 2009, pp. 77-95, doi : 10.1016 / S0065-2164 (08) 00804-6 . PMID 19203649 .