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Synonyms
cutinase, cutl1, cut190, fungal cutinase, thc_cut1, pet hydrolase, cutinase-like enzyme, lc-cutinase, cutinase 1, cdef1,
more
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4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
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4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
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4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
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cutin + H2O
cutin monomers
poly(epsilon-caprolactone) + H2O
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4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
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4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
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4-nitrophenyl hexanoate
4-nitrophenol + hexanoate
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4-nitrophenyl valerate
4-nitrophenol + pentanoate
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polybutylene succinate co-adipate + H2O
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additional information
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4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
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4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
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cutin + H2O
cutin monomers
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cutin + H2O
cutin monomers
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed
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additional information
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cutinases are capable of catalyzing esterification and transesterification
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additional information
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the cutinase demonstrates enhanced poly(epsilon-caprolactone) hydrolysis at high temperatures and under all pH value. The cutinase shows activity on 4-nitrophenyl butyrate
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evolution
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters
malfunction
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
physiological function
role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase
physiological function
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cutinases are hydrolytic enzymes that share properties of lipases and esterases, they are active regardless of the presence of an interface
physiological function
Aspergillus oryzae hydrophobin RolA adheres to the substrate polybutylene succinate co-adipate and promotes degradation by interacting with polyesterase CutL1 and recruiting it to the substrate surface. Residue D30 of CutL is involved in the CutL1-RolA interaction
physiological function
in a liquid medium containing the polybutylene succinate co-adipate, Aspergillus oryzae produces RolA, a hydrophobin, and cutinase CutL1, which degrades polybutylene succinate co-adipate. Secreted RolA attaches to the surface of the polybutylene succinate co-adipate particles and recruits CutL1. Residues Asp142, Asp171 and Glu31, located on the hydrophilic molecular surface of CutL1, and His32 and Lys34, located in the N-terminus of RolA, play crucial roles in the RolA-CutL1 interaction via ionic interactions
additional information
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent, the catalytic triad, formed by S126, H194, and D181, and key residues in the oxyanion hole, S48 and Q127
additional information
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biophysical parameters of cutinase as a function of pH, overview
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A102D/Q105R/G106E
pH-optima for activity and stability are identical to wild-type enzym. Improvement in Tm-value of 3.4°C. Increased half-life at 6°C relative to the wild-type enzyme of approximately 3fold
A102D/Q105R/G106E/N133A/S140P/E161T/A166P
large improvement of stability at 60°C
A102D/Q105R/G106E/N133A/S140P/E161T/A166P/K137E
large improvement of stability at 60°C
A102D/Q105R/G106E/Q98N/A99D/E109Q
thermodynamically most stable variant, improving on wild-type enzyme by 6.7 kJ/mol
A178P/V179P
loss of stability and activity
K174R/Y176F/A178E/D200R/G202E/D203E/D206R
mutant enzyme shows an increased kinetic stability
L26D/G28E/D30R/K67R
improvement in Tm-value of 0.7°C
N133A/S140P/E161T/A166P
proline mutations contribute to themostabilization by decreasing the entropy lost upon folding. Improvement in Tm of 1.7°C. Increased half-life at 6°C relative to the wild-type enzyme of approximately 2fold
Q110W/K114W
the mutant enzyme is retained in the endoplasmic reticulum whereas wild-type enzyme is secreted
R46P
the Tm-value is 3°C below that of wild-type enzyme
T84R/D86L/A99E/A100S
decrease in thermostability relative to the wild-type enzyme. Large losses in 4-nitrophenyl butyrate (about 70%) and poly(epsilon-caprolactone) (about 90%) activities
V150I/I136V
mutation do not provide any improvement in stability
D30S
mutation increases the KD value for interaction with hydrophobin RolA
D30S/E31S/D142S/D171S
mutation D30S increases the KD value for interaction with hydrophobin RolA in comparison with mutant E31S/D142S/D171S
additional information
mutational analysis toward the thermostabilization of the enzyme. Mutants with increased thermal unfolding temperature and increase in the half-life of the enzyme activity at 60°C do not display improved rate or temperature optimum of enzyme activity. Surface salt bridge optimization produces enthalpic stabilization. Mutations to proline reduces the entropy loss upon folding. The lack of a correlative increase in the temperature optimum of catalytic activity with thermodynamic stability suggests that the active site is locally denatured at a temperature below the thermal unfolding temperature of the global structure
additional information
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mutational analysis toward the thermostabilization of the enzyme. Mutants with increased thermal unfolding temperature and increase in the half-life of the enzyme activity at 60°C do not display improved rate or temperature optimum of enzyme activity. Surface salt bridge optimization produces enthalpic stabilization. Mutations to proline reduces the entropy loss upon folding. The lack of a correlative increase in the temperature optimum of catalytic activity with thermodynamic stability suggests that the active site is locally denatured at a temperature below the thermal unfolding temperature of the global structure
additional information
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because the organism has a low but significant FAE activity, it may be easier to introduce a high level of FAE activity in cutinases through point mutations
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Pio, T.; Macedo, G.
Cutinases: Properties and industrial applications
Adv. Appl. Microbiol.
66
77-95
2009
Aspergillus oryzae, Fusarium oxysporum, Fusarium solani, Humicola insolens
brenda
Liu, Z.; Gosser, Y.; Baker, P.J.; Ravee, Y.; Lu, Z.; Alemu, G.; Li, H.; Butterfoss, G.L.; Kong, X.P.; Gross, R.; Montclare, J.K.
Structural and functional studies of Aspergillus oryzae cutinase: enhanced thermostability and hydrolytic activity of synthetic ester and polyester degradation
J. Am. Chem. Soc.
131
15711-15716
2009
Aspergillus oryzae, Fusarium solani
brenda
Baker, P.; Poultney, C.; Liu, Z.; Gross, R.; Montclare, J.
Identification and comparison of cutinases for synthetic polyester degradation
Appl. Microbiol. Biotechnol.
93
229-240
2012
Aspergillus fumigatus, Aspergillus oryzae, Fusarium solani, Humicola insolens, Alternaria brassicicola
brenda
Chen, S.; Su, L.; Chen, J.; Wu, J.
Cutinase: characteristics, preparation, and application
Biotechnol. Adv.
31
1754-1767
2013
Alternaria brassicicola, Alternaria consortialis, Aspergillus nidulans (Q5AVY9), Aspergillus niger, Aspergillus oryzae (P52956), Bipolaris maydis, Botrytis cinerea (Q00298), Colletotrichum gloeosporioides, Colletotrichum gloeosporioides (P11373), Coprinopsis cinerea (B9U443), Cryptococcus sp. (in: Fungi) (Q874E9), Cryptococcus sp. (in: Fungi) S-2 (Q874E9), Fusarium oxysporum, Fusarium sambucinum, Fusarium solani (P00590), Helminthosporium sativum, Humicola insolens, Moesziomyces antarcticus (M9M134), Monilinia fructicola (Q2VF46), Penicillium citrinum, Penicillium sp., Pseudomonas aeruginosa, Pseudomonas mendocina, Pseudomonas putida, Pyrenopeziza brassicae (Q9Y7G8), Pyricularia grisea (P30272), Rhizoctonia solani, Streptomyces acidiscabies, Streptomyces badius, Streptomyces scabiei, Thermoactinomyces vulgaris, Thermobifida alba (E9LVH7), Thermobifida cellulosilytica (E9LVH8), Thermobifida cellulosilytica (E9LVH9), Thermobifida fusca, Thermobifida fusca DSM 44342, Thermothielavioides terrestris, Venturia inaequalis
brenda
Terauchi, Y.; Kim, Y.K.; Tanaka, T.; Nanatani, K.; Takahashi, T.; Abe, K.
Asp30 of Aspergillus oryzae cutinase CutL1 is involved in the ionic interaction with fungal hydrophobin RolA
Biosci. Biotechnol. Biochem.
81
1363-1368
2017
Aspergillus oryzae (I7GSC4), Aspergillus oryzae
brenda
Takahashi, T.; Tanaka, T.; Tsushima, Y.; Muragaki, K.; Uehara, K.; Takeuchi, S.; Maeda, H.; Yamagata, Y.; Nakayama, M.; Yoshimi, A.; Abe, K.
Ionic interaction of positive amino acid residues of fungal hydrophobin RolA with acidic amino acid residues of cutinase CutL1
Mol. Microbiol.
96
14-27
2015
Aspergillus oryzae (I7GSC4), Aspergillus oryzae
brenda
Shirke, A.N.; Basore, D.; Butterfoss, G.L.; Bonneau, R.; Bystroff, C.; Gross, R.A.
Toward rational thermostabilization of Aspergillus oryzae cutinase Insights into catalytic and structural stability
Proteins
84
60-72
2016
Aspergillus oryzae (P52956), Aspergillus oryzae, Aspergillus oryzae ATCC 42149 (P52956)
brenda
Aoyagi, H.; Katakura, Y.; Iwasaki, A.
Production of secretory cutinase by recombinant Saccharomyces cerevisiae protoplasts
SpringerPlus
5
1-6
2016
Aspergillus oryzae (P52956), Aspergillus oryzae ATCC 42149 (P52956)
brenda