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Literature summary for 3.5.1.117 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
Search for more literature for 3.5.1.117

Application

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

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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

Organism UniProt Comment Textmining
Agromyces sp. Q1EPR5
-
-
Agromyces sp. KY5R Q1EPR5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Agromyces sp.

Substrates and Products (Substrate)

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

Subunits Comment Organism
? 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

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

Temperature Stability [°C]

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

Turnover Number [1/s]

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