3.5.1.117: 6-aminohexanoate-oligomer endohydrolase
This is an abbreviated version!
For detailed information about 6-aminohexanoate-oligomer endohydrolase, go to the full flat file.
Word Map on EC 3.5.1.117
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3.5.1.117
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arthrobacter
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nylon-6
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flavobacterium
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6-aminohexanoate-dimer
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sitting-drop
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heterodimers
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vapour-diffusion
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amide
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unnatural
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compendium
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man-made
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orthorhombic
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byproduct
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tetramer
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agromyces
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hepes
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doughnut-shaped
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gel-filtration
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industry
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synthesis
- 3.5.1.117
- arthrobacter
- nylon-6
- flavobacterium
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6-aminohexanoate-dimer
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sitting-drop
- heterodimers
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vapour-diffusion
- amide
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unnatural
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compendium
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man-made
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orthorhombic
-
byproduct
- tetramer
- agromyces
- hepes
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doughnut-shaped
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gel-filtration
- industry
- synthesis
Reaction
Synonyms
6-aminohexanoate oligomer hydrolase, 6-aminohexanoate-dimer hydrolase, 6-aminohexanoate-hydrolase, 6-aminohexanoate-linear-dimer hydrolase, 6-aminohexanoate-oligomer hydrolase, 6-aminohexanoate-oligomer-hydrolase, 6-aminohexanoic acid-oligomer hydrolase, Ahx endo-type-oligomer hydrolase, Ahx oligomer hydrolase, Ahx-linear-dimer hydrolase, Ahx-oligomer hydrolase, AL2 hydrolase, Ald hydrolase, EII, endo-type 6-aminohexanoate oligomer hydrolase, endotype Ahx-oligomer hydrolase, NylB, NylB-type nylon-oligomer hydrolase, NylC, nylon hydrolase, nylon oligomer hydrolase, nylon oligomer-hydrolyzing enzyme, nylon-oligomer hydrolase, nylonase
ECTree
3.5.1.117 6-aminohexanoate-oligomer endohydrolaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.5.1.117 - 6-aminohexanoate-oligomer endohydrolase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-aminohexanoate oligomer + H2O
6-aminohexanoate dimer + ?
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-
-
?
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)7COOH + H2O
?
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600% activity compared to H2N(CH2)5CO-NH(CH2)5COOH
-
-
?
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
-
-
-
?
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
?
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
?
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
-
-
?
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
-
-
?
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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-
-
-
?
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
-
-
?
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
-
-
?
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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usage of nylon powders as substrates, nylon-6 is the preferred nyloln substrate
-
-
?
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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-
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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
-
-
?
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
-
-
?
