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6-aminohexanoate oligomer hydrolase
6-aminohexanoate-dimer hydrolase
6-aminohexanoate-hydrolase
6-aminohexanoate-linear-dimer hydrolase
6-aminohexanoate-oligomer hydrolase
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-
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6-aminohexanoate-oligomer-hydrolase
6-aminohexanoic acid-oligomer hydrolase
-
-
Ahx endo-type-oligomer hydrolase
Ahx-linear-dimer hydrolase
-
-
endo-type 6-aminohexanoate oligomer hydrolase
endotype Ahx-oligomer hydrolase
NylB-type nylon-oligomer hydrolase
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-
nylon oligomer-hydrolyzing enzyme
6-aminohexanoate oligomer hydrolase
-
6-aminohexanoate oligomer hydrolase
-
-
6-aminohexanoate-dimer hydrolase
-
-
6-aminohexanoate-dimer hydrolase
-
-
-
6-aminohexanoate-hydrolase
-
-
6-aminohexanoate-hydrolase
-
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6-aminohexanoate-hydrolase
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-
6-aminohexanoate-hydrolase
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-
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6-aminohexanoate-linear-dimer hydrolase
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-
6-aminohexanoate-linear-dimer hydrolase
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-
6-aminohexanoate-oligomer-hydrolase
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-
6-aminohexanoate-oligomer-hydrolase
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6-aminohexanoate-oligomer-hydrolase
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6-aminohexanoate-oligomer-hydrolase
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-
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Ahx endo-type-oligomer hydrolase
-
Ahx endo-type-oligomer hydrolase
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-
Ahx endo-type-oligomer hydrolase
-
Ahx endo-type-oligomer hydrolase
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-
Ahx-oligomer hydrolase
-
Ahx-oligomer hydrolase
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-
AL2 hydrolase
-
-
endo-type 6-aminohexanoate oligomer hydrolase
Q57326
-
endo-type 6-aminohexanoate oligomer hydrolase
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endotype Ahx-oligomer hydrolase
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endotype Ahx-oligomer hydrolase
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-
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NylB
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NylC
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nylon hydrolase
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nylon oligomer hydrolase
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nylon oligomer hydrolase
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nylon oligomer-hydrolyzing enzyme
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nylon oligomer-hydrolyzing enzyme
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-
nylon oligomer-hydrolyzing enzyme
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-
nylon oligomer-hydrolyzing enzyme
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nylon-oligomer hydrolase
-
nylon-oligomer hydrolase
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-
nylon-oligomer hydrolase
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-
nylon-oligomer hydrolase
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-
-
nylonase
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[N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
[N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
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-
-
-
[N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
NylB active site with a tyrosine residue Tyr170, cleavage mechanism of the Ald amide bond in acylation of NylB is as a two-step reaction, various intermediate states, catalytic mechanism, hybrid QM/MM dynamics in combination with free-energy sampling simulations, detailed overview
-
[N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
the Tyr170 residue points the NH group towards the proton-acceptor site of an artificial amide bond, reaction mechanism, overview
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[N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
NylB active site with a tyrosine residue Tyr170, cleavage mechanism of the Ald amide bond in acylation of NylB is as a two-step reaction, various intermediate states, catalytic mechanism, hybrid QM/MM dynamics in combination with free-energy sampling simulations, detailed overview
-
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[N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
the Tyr170 residue points the NH group towards the proton-acceptor site of an artificial amide bond, reaction mechanism, overview
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6-aminohexanoate cyclic oligomer + H2O
6-aminohexanoate
6-aminohexanoate cyclic oligomer + H2O
?
6-aminohexanoate oligomer + H2O
6-aminohexanoate dimer + ?
-
-
-
?
H2N(CH2)3CO-NH(CH2)5COOH + H2O
?
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4% activity compared to H2N(CH2)5CO-NH(CH2)5COOH
-
-
?
H2N(CH2)5CO-NH(CH2)3COOH + H2O
?
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15% activity compared to H2N(CH2)5CO-NH(CH2)5COOH
-
-
?
H2N(CH2)5CO-NH(CH2)5COOH + H2O
?
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100% activity
-
-
?
H2N(CH2)5CO-NH(CH2)7COOH + H2O
?
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600% activity compared to H2N(CH2)5CO-NH(CH2)5COOH
-
-
?
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
N-(6-aminohexanoyl)-N-(6-aminohexanoyl)-N-(6-aminohexanoyl)-6-aminohexanoate + H2O
N-(6-aminohexanoyl)-N-(6-aminohexanoyl)-6-aminohexanoate + N-(6-aminohexanoyl)-N-(6-aminohexanoate)-6-aminohexanoate
endo-type reaction
-
-
?
N-(6-aminohexanoyl)-N-(6-aminohexanoyl)-N-(6-aminohexanoyl)-N-(6-aminohexanoate)-6-aminohexanoate + H2O
N-(6-aminohexanoyl)-N-(6-aminohexanoyl)-6-aminohexanoate + N-(6-aminohexanoyl)-6-aminohexanoate
endo-type reaction
-
-
?
N-(6-aminohexanoyl)n-6-aminohexanoate + H2O
N-(6-aminohexanoyl)n-x + N-(6-aminohexanoyl)x-6-aminohexanoate
-
-
-
?
[N-(6-aminohexanoyl)]n + H2O
[N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
additional information
?
-
6-aminohexanoate cyclic oligomer + H2O
6-aminohexanoate
degree of polymerization > 3. The enzyme produces 6-aminohexanoate from Ahx cyclic oligomers (the NylC-specific substrate) but give no detectable amounts of reaction products from either the 6-aminohexanoate cyclic dimer or the 6-aminohexanoate linear dimer
-
-
?
6-aminohexanoate cyclic oligomer + H2O
6-aminohexanoate
degree of polymerization > 3. The enzyme produces 6-aminohexanoate from Ahx cyclic oligomers (the NylC-specific substrate) but give no detectable amounts of reaction products from either the 6-aminohexanoate cyclic dimer or the 6-aminohexanoate linear dimer
-
-
?
6-aminohexanoate cyclic oligomer + H2O
?
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-
-
?
6-aminohexanoate cyclic oligomer + H2O
?
degree of polymerization > 3. The enzyme produces 6-aminohexanoate from Ahx cyclic oligomers (the NylC-specific substrate) but give no detectable amounts of reaction products from either the 6-aminohexanoate cyclic dimer or the 6-aminohexanoate linear dimer
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-
?
6-aminohexanoate cyclic oligomer + H2O
?
degree of polymerization > 3. The enzyme produces 6-aminohexanoate from Ahx cyclic oligomers (the NylC-specific substrate) but give no detectable amounts of reaction products from either the 6-aminohexanoate cyclic dimer or the 6-aminohexanoate linear dimer
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-
?
6-aminohexanoate cyclic oligomer + H2O
?
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?
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
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synthesis method, overview
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?
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
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synthesis method, overview
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?
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
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synthesis method, overview
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?
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
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synthesis method, overview
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?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
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?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
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?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
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?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
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?
nylon oligomer + H2O
?
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?
nylon oligomer + H2O
?
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?
nylon oligomer + H2O
?
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?
nylon oligomer + H2O
?
endo-type reaction. Linear oligomers of 6-aminohexanoate such as the tetramer and the pentamer are initially produced and subsequently converted to smaller oligomers such as the dimer. The enzyme predominantly cleaves amide bonds located at the second and third positions from the carbobenzoxy group. This enzyme favors a longer chain of linear oligomer digesting the internal amide bonds preferentially but has no activity toward N-(6-aminohexanoyl)-6-aminohexanoate or 6-aminohexanoate cyclic dimer
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?
nylon oligomer + H2O
?
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?
nylon oligomer + H2O
?
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?
nylon-6 + H2O
?
enzymatic hydrolysis of nylon-6 by a thermostable NylC mutant. The enzyme hydrolyzes nylon, but the fragments that are produced are still bound to polymer chains through hydrogen bonding. The fragments correspond to oligomers with 13-25 monomeric units. The N-terminal Thr-267 of the 9-kDa subunit is the catalytic residue. The smaller fragents (<10 monomeric subunits) are released from the solid fraction
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?
nylon-6 + H2O
?
enzymatic hydrolysis of nylon-6 by a thermostable NylC mutant. The enzyme hydrolyzes nylon, but the fragments that are produced are still bound to polymer chains through hydrogen bonding. The fragments correspond to oligomers with 13-25 monomeric units. The N-terminal Thr-267 of the 9-kDa subunit is the catalytic residue. The smaller fragents (<10 monomeric subunits) are released from the solid fraction
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?
nylon-6 polymer + H2O
?
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nylon-6 is the preferred nyloln substrate
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?
nylon-6 polymer + H2O
?
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usage of nylon powders as substrates, nylon-6 is the preferred nyloln substrate
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?
nylon-6 polymer + H2O
?
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?
nylon-6 polymer + H2O
?
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?
nylon-66 polymer + H2O
?
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identification of the reaction product from the nylon-(66-co-64(0.32)) copolymer by nylon hydrolase
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?
nylon-66 polymer + H2O
?
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usage of nylon powders as substratesm, nylon-66 is hydrolyzed by the hydrolase, although the extent of degradation of nylon-66 is approximately 60% of that for nylon-6. Identification of the reaction product from the nylon-(66-co-64(0.32)) copolymer by nylon hydrolase
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?
[N-(6-aminohexanoyl)]n + H2O
[N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
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linear Ahx-dimer, Ahx-trimer, and Ahx-tetramer, as well as Ahx-linear oligomer, and Ahx-cyclic dimer
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?
[N-(6-aminohexanoyl)]n + H2O
[N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
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?
[N-(6-aminohexanoyl)]n + H2O
[N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
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?
[N-(6-aminohexanoyl)]n + H2O
[N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
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?
additional information
?
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NylCp2 hydrolyzes Ahx cyclic and linear oligomers (degree of polymerization of more than 3) but has no detectable activity with D,L-Ala-Gly-Gly
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?
additional information
?
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NylCp2 hydrolyzes Ahx cyclic and linear oligomers (degree of polymerization of more than 3) but has no detectable activity with D,L-Ala-Gly-Gly
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?
additional information
?
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nylon hydrolase degrades various aliphatic nylons, including nylon-6 and nylon-66. Nylons are synthetic polymers made from (a) a dicarboxylic acid and a diamine (e.g., for nylon-66 production), (b) an amino acid that is able to undergo self-condensation, or (c) its lactam, such as epsilon-caprolactam (for nylon-6 production). The enzyme reaction proceeds by degrading the solid polymer to soluble oligomers (step 1), followed by degrading the released soluble oligomers into smaller oligomers and/or monomers (step 2). During the polymer degradations, these two steps should proceed simultaneously. Nylon hydrolase (NylC) attacks the polymer chains that are exposed to the solvent, especially at positions where hydrogen-bonding between the polymer chains is partially weakened
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?
additional information
?
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development and evaluation of an assay method that enables a quantitative evaluation of the reaction rate of hydrolysis at the interface between the solid and aqueous phases and a quantitative comparison of the degradability for various polyamides, overview. Thin layer product identification
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?
additional information
?
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NylCp2 hydrolyzes Ahx cyclic and linear oligomers (degree of polymerization of more than 3) but has no detectable activity with D,L-Ala-Gly-Gly
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?
additional information
?
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negligible activity with N-(6-aminohexanoyl)-6-aminohexanoate and N-(6-aminohexanoyl)-N-(6-aminohexanoyl)-6-aminohexanoate and the cyclic dimer 1,8-diazacyclotetradecane-2,9-dione
-
-
?
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0.5 - 2
N-(4-nitrophenyl)-6-aminohexanamide
0.6 - 15
N-(6-aminohexanoyl)-6-aminohexanoate
additional information
6-aminohexanoate cyclic oligomer
0.5
N-(4-nitrophenyl)-6-aminohexanamide
-
pH and temperature not specified in the publication
2
N-(4-nitrophenyl)-6-aminohexanamide
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pH and temperature not specified in the publication
0.6
N-(6-aminohexanoyl)-6-aminohexanoate
-
pH and temperature not specified in the publication
15
N-(6-aminohexanoyl)-6-aminohexanoate
-
pH and temperature not specified in the publication
additional information
6-aminohexanoate cyclic oligomer
KM 6-aminohexanoate cyclic oligomer: 3.7 mg/ml, pH 7.3, 60°C, mutant enzyme D122G/H130Y/D36A/E236Q
additional information
6-aminohexanoate cyclic oligomer
-
KM 6-aminohexanoate cyclic oligomer: 3.7 mg/ml, pH 7.3, 60°C, mutant enzyme D122G/H130Y/D36A/E236Q
additional information
6-aminohexanoate cyclic oligomer
Km-value for 6-aminohexanoate cyclic oligomer: 0.44 mg/ml, pH 7.0, 30°C
additional information
6-aminohexanoate cyclic oligomer
Km-value for 6-aminohexanoate cyclic oligomer: 0.49 mg/ml, pH 7.0, 30°C
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metabolism
enzymatic degradation of 6-aminohexanoate and its oligomers in Arthrobacter sp. KI7 by the Nyl enzymes. A 6-aminohexanoate oligomer is converted to adipate, pathway overview. 6-Aminohexanoate oligomers are almost completely converted to the monomers (Ahx) by the three nylon oligomer-degrading enzymes, NylA, NylB, and NylC. 6-Aminohexanoate aminotransferase (NylD1) catalyzes the reaction of 6-aminohexanoate to adipate semialdehyde using alpha-ketoglutarate, pyruvate, and glyoxylate as amino acceptors, generating glutamate, alanine, and glycine, respectively. The reaction requires pyridoxal phosphate (PLP) as a cofactor. For further metabolism, adipate semialdehyde dehydrogenase (NylE1) catalyzes the oxidative reaction of adipate semialdehyde to adipate using NADP+ as a cofactor
evolution
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enzyme NylC is a member of the N-terminal nucleophile hydrolase superfamily
evolution
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NylB belongs to the class C of the beta-lactamase family, which is characterized by the presence of a catalytic triad, namely, Ser, Tyr, and Lys, having the ability to promote the hydrolysis of amide and/or ester bonds. Natural selection is responsible for the development of the peculiar hydrolytic activity of Arthrobacter sp. KI72
evolution
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the active site of 6-aminohexanoate-dimer hydrolase, a nylon-6 byproduct-degrading enzyme with a beta-lactamase fold, possesses a Ser112/Lys115/Tyr215 catalytic triad similar to the one of penicillin-recognizing family of serine-reactive hydrolases but includes a unique Tyr170 residue. Three types of nylon-oligomer hydrolases: Ahx-cyclic-dimer hydrolase exist: (NylA), Ahx-linear-dimer (Ald) hydrolase (NylB), and endotype Ahx-oligomer hydrolase (NylC)
evolution
-
the active site of 6-aminohexanoate-dimer hydrolase, a nylon-6 byproduct-degrading enzyme with a beta-lactamase fold, possesses a Ser112/Lys115/Tyr215 catalytic triad similar to the one of penicillin-recognizing family of serine-reactive hydrolases but includes a unique Tyr170 residue. Three types of nylon-oligomer hydrolases: Ahx-cyclic-dimer hydrolase exist: (NylA), Ahx-linear-dimer (Ald) hydrolase (NylB), and endotype Ahx-oligomer hydrolase (NylC)
-
evolution
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NylB belongs to the class C of the beta-lactamase family, which is characterized by the presence of a catalytic triad, namely, Ser, Tyr, and Lys, having the ability to promote the hydrolysis of amide and/or ester bonds. Natural selection is responsible for the development of the peculiar hydrolytic activity of Arthrobacter sp. KI72
-
additional information
-
the active site of 6-aminohexanoate-dimer hydrolase, a nylon-6 byproduct-degrading enzyme with a beta-lactamase fold, possesses a Ser112/Lys115/Tyr215 catalytic triad similar to the one of penicillin-recognizing family of serinereactive hydrolases but includes a unique Tyr170 residue
additional information
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the enzyme can adopt two different conformations: a substrate-free form (open form) and a substrate-bound form (closed from), hybrid quantum mechanics/molecular mechanics (QM/MM) dynamical simulations complemented with free energy sampling methods, allow to determine the reaction mechanismin NylB and address one of the possible roles of Tyr170 during the acylation process, enzyme structure and induced-fit process, detailed overview
additional information
-
the enzyme can adopt two different conformations: a substrate-free form (open form) and a substrate-bound form (closed from), hybrid quantum mechanics/molecular mechanics (QM/MM) dynamical simulations complemented with free energy sampling methods, allow to determine the reaction mechanismin NylB and address one of the possible roles of Tyr170 during the acylation process, enzyme structure and induced-fit process, detailed overview
additional information
-
the active site of 6-aminohexanoate-dimer hydrolase, a nylon-6 byproduct-degrading enzyme with a beta-lactamase fold, possesses a Ser112/Lys115/Tyr215 catalytic triad similar to the one of penicillin-recognizing family of serinereactive hydrolases but includes a unique Tyr170 residue
-
additional information
-
the enzyme can adopt two different conformations: a substrate-free form (open form) and a substrate-bound form (closed from), hybrid quantum mechanics/molecular mechanics (QM/MM) dynamical simulations complemented with free energy sampling methods, allow to determine the reaction mechanismin NylB and address one of the possible roles of Tyr170 during the acylation process, enzyme structure and induced-fit process, detailed overview
-
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27408
x * 27408 + x * 9513, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, calculation from nucleotide sequence
31000
x * 31000 + x * 9000, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, SDS-PAGE
9513
x * 27408 + x * 9513, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, calculation from nucleotide sequence
27000
4 * (1 * 27000 + 1 * 9000), four identical heterodimers (27 kDa + 9 kDa), which result from the autoprocessing of the precursor protein (36 kDa) constitute the doughnut-shaped quaternary structure, each heterodimer is folded into a single domain, generating a stacked alpha,beta,beta,alpha core structure
27000
x * 27000 + x * 9000, SDS-PAGE
27000
x * 27000 + x * 9000, SDS-PAGE
27000
-
1 * 27000 + 1 * 9000, SDS-PAGE
9000
x * 27000 + x * 9000, SDS-PAGE
9000
x * 27000 + x * 9000, SDS-PAGE
9000
x * 31000 + x * 9000, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, SDS-PAGE
9000
-
1 * 27000 + 1 * 9000, SDS-PAGE
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?
4 * (1 * 27000 + 1 * 9000), four identical heterodimers (27 kDa + 9 kDa), which result from the autoprocessing of the precursor protein (36 kDa) constitute the doughnut-shaped quaternary structure, each heterodimer is folded into a single domain, generating a stacked alpha,beta,beta,alpha core structure
?
x * 27000 + x * 9000, SDS-PAGE
?
-
x * 27000 + x * 9000, SDS-PAGE
-
?
-
4 * (1 * 27000 + 1 * 9000), four identical heterodimers (27 kDa + 9 kDa), which result from the autoprocessing of the precursor protein (36 kDa) constitute the doughnut-shaped quaternary structure, each heterodimer is folded into a single domain, generating a stacked alpha,beta,beta,alpha core structure
-
?
x * 27408 + x * 9513, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, calculation from nucleotide sequence
?
x * 31000 + x * 9000, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, SDS-PAGE
?
x * 27000 + x * 9000, SDS-PAGE
?
-
x * 27000 + x * 9000, SDS-PAGE
-
heterodimer
-
1 * 27000 + 1 * 9000, SDS-PAGE
heterodimer
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1 * 27000 + 1 * 9000, SDS-PAGE
-
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D122G
mutation increases the melting temperature by 24°C compared to wild-type enzyme
D122G/H130Y
mutation increases the melting temperature by 29°C compared to wild-type enzyme
D122G/H130Y/D36A
mutation increases the melting temperature by 32°C compared to wild-type enzyme
D122G/H130Y/D36A/E236Q
mutation increases the melting temperature by 36°C compared to wild-type enzyme
D122G/H130Y/E263Q
mutation increases the melting temperature by 32°C compared to wild-type enzyme
D122G/H130Y/L137A
mutation increases the melting temperature by 2°C compared to wild-type enzyme
G111S
mutation decreases the melting temperature by 9°C compared to wild-type enzyme
G111S/D122G/H130Y
mutation increases the melting temperature by 26°C compared to wild-type enzyme
G111S/D122G/H130Y/L137A
mutation decreases the melting temperature by 1°C compared to wild-type enzyme
H130Y
mutation increases the melting temperature by 11°C compared to wild-type enzyme
L137A
mutation decreases the melting temperature by 11°C compared to wild-type enzyme
D122G
-
mutation increases the melting temperature by 24°C compared to wild-type enzyme
-
D122G/H130Y/D36A/E263Q
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mutations enhance the protein thermostability by 36°C (melting temperature: 88°C). More than 90% of the enzyme activity is retained after incubation of the mutant for 30 min at 70°C
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G111S
-
mutation decreases the melting temperature by 9°C compared to wild-type enzyme
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H130Y
-
mutation increases the melting temperature by 11°C compared to wild-type enzyme
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L137A
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mutation decreases the melting temperature by 11°C compared to wild-type enzyme
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D15G
-
site-directed mutagenesis
D181G
-
site-directed mutagenesis
G181D/H266N
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site-directed mutagenesis
G181D/H266N/D370Y
-
site-directed mutagenesis
P4R
-
site-directed mutagenesis
S8Q
-
site-directed mutagenesis
T3A
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site-directed mutagenesis
T5S
-
site-directed mutagenesis
Y170F
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site-directed mutagenesis, the Tyr170 is replaced by phenylalanine, which is unable to form a hydrogen bond with the amide bond, thus, resulting in an increase in the activation barrier of more than 10 kcal/mol, but despite the lack of hydrogen bonding between the Y170F and the substrate, the highest free energy barrier for the induced-fit is similar to that of wild-type suggesting that in the induced-fit process, kinetics is little affected by the mutation, hybrid quantum mechanics/molecular mechanics (QM/MM) dynamical simulations
D15G
-
site-directed mutagenesis
-
D181G
-
site-directed mutagenesis
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P4R
-
site-directed mutagenesis
-
T3A
-
site-directed mutagenesis
-
Y170F
-
site-directed mutagenesis, the Tyr170 is replaced by phenylalanine, which is unable to form a hydrogen bond with the amide bond, thus, resulting in an increase in the activation barrier of more than 10 kcal/mol, but despite the lack of hydrogen bonding between the Y170F and the substrate, the highest free energy barrier for the induced-fit is similar to that of wild-type suggesting that in the induced-fit process, kinetics is little affected by the mutation, hybrid quantum mechanics/molecular mechanics (QM/MM) dynamical simulations
-
D122G/H130Y/D36A/E263Q
mutations enhance the protein thermostability by 36°C (melting temperature: 88°C). More than 90% of the enzyme activity is retained after incubation of the mutant for 30 min at 70°C
D122G/H130Y/D36A/E263Q
-
site-directed mutagenesis, the mutant enzyme hydrolyzes polymeric nylon-6 powder, but the extent of the degradation is low
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Paenarthrobacter ureafaciens (P07062)
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