3.1.1.74: cutinase
This is an abbreviated version!
For detailed information about cutinase, go to the full flat file.
Word Map on EC 3.1.1.74
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3.1.1.74
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fusarium
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solani
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pi
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lipase
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terephthalate
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p-nitrophenyl
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lipolytic
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thermobifida
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esterases
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insolens
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fusca
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humicola
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ideonella
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polybutylene
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sakaiensis
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industry
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polycaprolactone
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tributyrin
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degradation
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sulfosuccinate
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haematococca
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monilinia
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terephthalic
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petase
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synthesis
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nectria
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hydrophobins
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saccharomonospora
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biotechnology
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environmental protection
- 3.1.1.74
- fusarium
- solani
- pi
- lipase
- terephthalate
- p-nitrophenyl
-
lipolytic
- thermobifida
- esterases
- insolens
- fusca
-
humicola
-
ideonella
-
polybutylene
- sakaiensis
- industry
-
polycaprolactone
- tributyrin
- degradation
- sulfosuccinate
- haematococca
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monilinia
-
terephthalic
- petase
- synthesis
- nectria
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hydrophobins
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saccharomonospora
- biotechnology
- environmental protection
Reaction
Synonyms
acidic cutinase, CcCUT1, CDEF1, CLE, Cut 5a, cut-2.KW3, Cut1, Cut11, Cut190, Cut2, Cut5a, CUTAB1, CutB, cuticle destructing factor 1, cutin esterase, cutin hydrolase, cutinase, cutinase 1, cutinase 2, cutinase-1, cutinase-like enzyme, cutinolytic polyesterase, CutL, CutL1, FspC, fungal cutinase, HIc, LC-cutinase, More, MYCTH_2110987, PET hydrolase, Tfu_0883, Thcut1, THCUT1 protein, Thc_Cut1, Thc_Cut2, TRIREDRAFT_60489
ECTree
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General Information
General Information on EC 3.1.1.74 - cutinase
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evolution
malfunction
physiological function
additional information
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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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
evolution
Helminthosporium sativum
-
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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. The cutinase from Thermobifida alba also adopts an alpha/beta fold, but it is larger than the ones from other family members. It contains nine sheets at the heart of the protein, two of which are antiparallel, rather than the five parallel sheets present in the fungal enzymes
evolution
modeling and comparison of the structures of the two closely related cutinases Thc_Cut1 and Thc_Cut2 from Thermobifida cellulosilytica DSM44535 reveal that dissimilarities in their electrostatic and hydrophobic surface properties in the vicinity to the active site might be responsible for pronounced differences in hydrolysis efficiencies of polyester (i.e., PET, polyethyleneterephthalate), isozyme Thc_Cut2 hydrolyzes PET much less efficiently than Thc_Cut1
evolution
modeling and comparison of the structures of the two closely related cutinases Thc_Cut1 and Thc_Cut2 from Thermobifida cellulosilytica DSM44535 reveal that dissimilarities in their electrostatic and hydrophobic surface properties in the vicinity to the active site might be responsible for pronounced differences in hydrolysis efficiencies of polyester (i.e., PET, polyethyleneterephthalate), Thc_Cut2 hydrolyzes PET much less efficiently than Thc_Cut1
evolution
residues N168, Q170 an N171 of Glomerella cingulata are highly conserved with all cutinases of fungal phytopathogens
evolution
the enzyme contains the conserved motif G-Y-S-Q-G surrounding the active site serine as well as the aspartic acid and histidine residues of the cutinase active site
evolution
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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
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evolution
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the enzyme contains the conserved motif G-Y-S-Q-G surrounding the active site serine as well as the aspartic acid and histidine residues of the cutinase active site
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evolution
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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
-
evolution
-
modeling and comparison of the structures of the two closely related cutinases Thc_Cut1 and Thc_Cut2 from Thermobifida cellulosilytica DSM44535 reveal that dissimilarities in their electrostatic and hydrophobic surface properties in the vicinity to the active site might be responsible for pronounced differences in hydrolysis efficiencies of polyester (i.e., PET, polyethyleneterephthalate), isozyme Thc_Cut2 hydrolyzes PET much less efficiently than Thc_Cut1
-
evolution
-
modeling and comparison of the structures of the two closely related cutinases Thc_Cut1 and Thc_Cut2 from Thermobifida cellulosilytica DSM44535 reveal that dissimilarities in their electrostatic and hydrophobic surface properties in the vicinity to the active site might be responsible for pronounced differences in hydrolysis efficiencies of polyester (i.e., PET, polyethyleneterephthalate), Thc_Cut2 hydrolyzes PET much less efficiently than Thc_Cut1
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specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
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specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
-
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
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specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
-
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
-
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
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specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
-
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
-
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
-
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
Helminthosporium sativum
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specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
-
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
-
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
CDEF1 is a plant cutinase, recombinant CDEF1 protein has esterase activity. Ectopic expression of CDEF1 driven by the 35S promoter causes fusion of organs, including leaves, stems and flowers, and increased surface permeability. CDEF1 is involved in the penetration of the stigma by pollen tubes. CDEF1 degrades cell wall components to facilitate the emergence of the lateral roots
physiological function
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contains four cutinase genes, which may result from its low repetitive content and mild form of repeat induced point mutation
physiological function
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contains three cutinases, which show less than 80% sequence identity, indicating that they are duplicated and diverged before the emergence of the active repeat induced point mutation defence mechanism, and have been retained in the genome by virtue of their varying regulatory or functional diversity
physiological function
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cutinases are hydrolytic enzymes that share properties of lipases and esterases, and also display the unique characteristic of being active regardless of the presence of an interface
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
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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
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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
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ectopic expression of CDEF1 driven by the 35S promoter causes fusion of organs, including leaves, stems and flowers, and increased surface permeability
physiological function
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the organism contains 11 cutinases, despite the 3-4% repetitive DNA content and the repeat induced point mutation-based elimination of transposable elements
physiological function
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the organism contains 12 cutinases. High number of cutinases likely reflects its needs during post-invasion necrotrophic growth and overwintering as saprotrophic mycelia, and its ability to infect many different monocotyledonous genera asymptomatically
physiological function
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the organism contains 17 cutinases. Preservation of a large number of diverse cutinases within the genome may provide the fungus with a great selective advantage to breach multiple, diverse grass cuticles, or may reflect its requirements to degrade different plant debris while overwintering as a soil saprotroph
physiological function
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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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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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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
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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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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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
-
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
-
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
-
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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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
-
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
Helminthosporium sativum
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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
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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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
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
-
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
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
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
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
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
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
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
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
the enzyme is an elicitor that triggers defense responses in plants, recombinant His-tagged enzyme causes cell death in Arabidopsis thaliana, Glycine max, Brassica napus, Oryza sativa, Zea mays, and Triticum aestivum, indicating that both dicot and monocot species are responsive to the elicitor. The elicitation of Nicotiana tabacum is effective in the induction of the activities of hydrogen peroxide, phenylalanine ammonia-lyase, peroxides, and polyphenol oxidase. Phenotypes, detailed overview
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
expression of cutinase fused to pelB signal peptide in a secB knockout strain, defective in type II secretion pathway, still leads to accumulation of cutinase in the culture medium. The phospholipid hydrolase activity of pelB-cutinase plays a role in its extracellular production
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
physiological function
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isoform CUT11 protein induces cell death and triggers defense responses in Nicotiana benthamiana, cotton, and tomato plants. CUT11 induces plant defense responses in Nicotiana benthamania in a BAK1 and SOBIR-dependent manner. The carbohydrate-binding module family 1 protein suppresses CUT11-induced cell death and other defense responses in Nicothiana benthamiana
physiological function
Verticillium dahliae Vd991
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isoform CUT11 protein induces cell death and triggers defense responses in Nicotiana benthamiana, cotton, and tomato plants. CUT11 induces plant defense responses in Nicotiana benthamania in a BAK1 and SOBIR-dependent manner. The carbohydrate-binding module family 1 protein suppresses CUT11-induced cell death and other defense responses in Nicothiana benthamiana
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biophysical parameters of cutinase as a function of pH, overview
additional information
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biophysical parameters of cutinase as a function of pH, overview
additional information
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biophysical parameters of cutinase as a function of pH, overview
additional information
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biophysical parameters of cutinase as a function of pH, overview
additional information
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biophysical parameters of cutinase as a function of pH, overview
additional information
residues Ser117, Asp169, and His182 form the active site
additional information
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residues Ser117, Asp169, and His182 form the active site
additional information
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residues Ser165, Asp210, and His242 form the catalytic triad. The disulfide bond formed by Cys275 and Cys292 contributes not only to the thermodynamic stability but also to the kinetic stability of LC-cutinase
additional information
structure analysis, structure comparisons of isozymes Cut1 and Cut2 during denaturation and unfolding, homology modeling, overview
additional information
structure analysis, structure comparisons of isozymes Cut1 and Cut2 during denaturation and unfolding, homology modeling, overview
additional information
structure-activity relationship analysis, active site structure, the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent, the catalytic triad, formed by S120, H188, D175, and key residues in the oxyanion hole, S42 and Q121, are important for stabilizing the transitions states in the acylation/deacylation steps of the enzyme mechanism
additional information
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the enzyme has a Ser130-His208-Asp176 catalytic triad in which Ser130 is critical to the hydrolytic activity
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
Helminthosporium sativum
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
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
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent, the catalytic triad, formed by S169, H247, and D215, and key residues in the oxyanion hole, M179 and Y99, active site structure, overview
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 S85, H180, and D165, and key residues in the oxyanion hole, T17 and Q86
additional information
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Residues S103 and H173 from Monilinia fructicola cutinase play important roles in catalysis
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. The conformation of the Glomerella cingulata catalytic triad appears to cycle between an inactive form and an active form during catalysis. In the uninhibited structure, the histidine residue that forms the center of the catalytic triad is positioned outside of the active site, and does not interact with the remainder of the triad, catalytic serine and catalytic aspartate. In addition, there is a small helix in the vicinity of the active site that places the catalytic serine in a deep hole in a deep pocketwithin the active site
additional information
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. The conformation of the Glomerella cingulata catalytic triad appears to cycle between an inactive form and an active form during catalysis. In the uninhibited structure, the histidine residue that forms the center of the catalytic triad is positioned outside of the active site, and does not interact with the remainder of the triad, catalytic serine and catalytic aspartate. In addition, there is a small helix in the vicinity of the active site that places the catalytic serine in a deep hole in a deep pocketwithin the active site
additional information
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
additional information
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
additional information
E5BBQ3
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
additional information
E9LVI0
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
additional information
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent, the catalytic triad, formed by S85, H180, and D165, and key residues in the oxyanion hole, T17 and Q86
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additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
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