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Literature summary extracted from

  • Negoro, S.; Shibata, N.; Tanaka, Y.; Yasuhira, K.; Shibata, H.; Hashimoto, H.; Lee, Y.H.; Oshima, S.; Santa, R.; Oshima, S.; Mochiji, K.; Goto, Y.; Ikegami, T.; Nagai, K.; Kato, D.; Takeo, M.; Higuchi, Y.
    Three-dimensional structure of nylon hydrolase and mechanism of nylon-6 hydrolysis (2012), J. Biol. Chem., 287, 5079-5090.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.5.1.117 industry the partial enzymatic hydrolysis of nylon surfaces by NylC can be used to change the smoothness of nylon fibers Agromyces sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.117 expressed in Escherichia coli JM109 cells Agromyces sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.117 sitting drop vapor diffusion method, using 1.0 M sodium citrate as a precipitant in 0.1 M HEPES buffer (pH 7.5), 0.2 M NaCl Agromyces sp.

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.117 D122G mutation increases the melting temperature by 24°C compared to wild-type enzyme Agromyces sp.
3.5.1.117 D122G/H130Y mutation increases the melting temperature by 29°C compared to wild-type enzyme Agromyces sp.
3.5.1.117 D122G/H130Y/D36A mutation increases the melting temperature by 32°C compared to wild-type enzyme Agromyces sp.
3.5.1.117 D122G/H130Y/D36A/E236Q mutation increases the melting temperature by 36°C compared to wild-type enzyme Agromyces sp.
3.5.1.117 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 Agromyces sp.
3.5.1.117 D122G/H130Y/E263Q mutation increases the melting temperature by 32°C compared to wild-type enzyme Agromyces sp.
3.5.1.117 D122G/H130Y/L137A mutation increases the melting temperature by 2°C compared to wild-type enzyme Agromyces sp.
3.5.1.117 G111S mutation decreases the melting temperature by 9°C compared to wild-type enzyme Agromyces sp.
3.5.1.117 G111S/D122G/H130Y mutation increases the melting temperature by 26°C compared to wild-type enzyme Agromyces sp.
3.5.1.117 G111S/D122G/H130Y/L137A mutation decreases the melting temperature by 1°C compared to wild-type enzyme Agromyces sp.
3.5.1.117 H130Y mutation increases the melting temperature by 11°C compared to wild-type enzyme Agromyces sp.
3.5.1.117 L137A mutation decreases the melting temperature by 11°C compared to wild-type enzyme Agromyces sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.117 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 Agromyces sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.117 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 Agromyces sp.

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.117 Agromyces sp. Q1EPR5
-
-
3.5.1.117 Agromyces sp. KY5R Q1EPR5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.117
-
 Agromyces sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.117 6-aminohexanoate cyclic oligomer + H2O
-
 Agromyces sp. ?
-
 ?
3.5.1.117 6-aminohexanoate cyclic oligomer + H2O
-
 Agromyces sp. KY5R ?
-
 ?
3.5.1.117 additional information 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 Agromyces sp. ?
-
 ?
3.5.1.117 additional information 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 Agromyces sp. KY5R ?
-
 ?
3.5.1.117 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 Agromyces sp. ?
-
 ?
3.5.1.117 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 Agromyces sp. KY5R ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.117 ? 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 Agromyces sp.

Synonyms

EC Number Synonyms Comment Organism
3.5.1.117 6-aminohexanoate oligomer hydrolase
-
 Agromyces sp.
3.5.1.117 NylC
-
 Agromyces sp.
3.5.1.117 nylon hydrolase
-
 Agromyces sp.
3.5.1.117 nylonase
-
 Agromyces sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.117 41
-
 melting temperature of of mutant enzyme L137A Agromyces sp.
3.5.1.117 43
-
 melting temperature of of mutant enzyme G111S Agromyces sp.
3.5.1.117 51
-
 melting temperature of mutant enzyme G111S/D122G/H130Y/L137A Agromyces sp.
3.5.1.117 52
-
 melting temperature of wild type enzyme Agromyces sp.
3.5.1.117 54
-
 melting temperature of mutant enzyme D122G/H130Y/L137A Agromyces sp.
3.5.1.117 60
-
 melting temperature of the mutant enzyme G111S/D122G/H130Y/L137A/V225M is 60°C Agromyces sp.
3.5.1.117 63
-
 melting temperature of mutant enzyme H130Y Agromyces sp.
3.5.1.117 63
-
 melting temperature of of mutant enzyme H130Y Agromyces sp.
3.5.1.117 70
-
 30 min, more than 90% of enzyme activity of mutant D122G/H130Y/D36A/E263Q is retained Agromyces sp.
3.5.1.117 76
-
 melting temperature of mutant enzyme D122G Agromyces sp.
3.5.1.117 76
-
 melting temperature of of mutant enzyme D122G Agromyces sp.
3.5.1.117 78
-
 melting temperature of mutant enzyme G111S/D122G/H130Y Agromyces sp.
3.5.1.117 81
-
 melting temperature of of mutant enzyme D122G/H130Y Agromyces sp.
3.5.1.117 83
-
 melting temperature of mutant enzyme D122G/H130Y/V225M Agromyces sp.
3.5.1.117 84
-
 melting temperature of mutant enzyme D122G/H130Y/D36A or D122G/H130Y/E263Q Agromyces sp.
3.5.1.117 88
-
 melting temperature of mutant D122G/H130Y/D36A/E263Q Agromyces sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.117 6.5
-
 6-aminohexanoate cyclic oligomer pH 7.3, 60°C, mutant enzyme D122G/H130Y/D36A/E236Q Agromyces sp.