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EC Tree
IUBMB Comments The enzyme is involved in degradation of nylon-6 oligomers. It degrades linear oligomers of 6-aminohexanoate with a degree of polymerization of 2--20 by exo-type cleavage, removing residues sequentially from the N-terminus. Activity decreases with the increase of the polymerization number of the oligomer. cf. EC 3.5.1.117, 6-aminohexanoate-oligomer endohydrolase and EC 3.5.2.12, 6-aminohexanoate-cyclic-dimer hydrolase.
The taxonomic range for the selected organisms is: Flavobacterium sp. The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
6-aminohexanoate-dimer hydrolase, hyb-24, nylon oligomer hydrolase, 6-aminohexanoate dimer hydrolase, nylcp2, hyb-24dn, 6-aminohexanoate oligomer hydrolase,
more
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nylon-oligomer degrading enzyme
-
6-aminohexanoate-dimer hydrolase
-
-
-
-
6-aminohexanoic acid oligomer hydrolase
-
-
-
-
N-(6-aminohexanoyl)-6-aminohexanoate amidohydrolase
-
-
-
-
Nylon oligomers degrading enzyme EII
-
-
-
-
Nylon oligomers degrading enzyme EII'
-
-
-
-
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hydrolysis of peptide bond
-
-
-
-
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N-(6-aminohexanoyl)-6-aminohexanoate exoamidohydrolase
The enzyme is involved in degradation of nylon-6 oligomers. It degrades linear oligomers of 6-aminohexanoate with a degree of polymerization of 2--20 by exo-type cleavage, removing residues sequentially from the N-terminus. Activity decreases with the increase of the polymerization number of the oligomer. cf. EC 3.5.1.117, 6-aminohexanoate-oligomer endohydrolase and EC 3.5.2.12, 6-aminohexanoate-cyclic-dimer hydrolase.
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N-(4-aminobutyryl)-4-aminobutyric acid + H2O
4-aminobutyric acid + 4-aminobutyric acid
-
very low activity for EII
-
?
N-(6-aminohexanoyl)-4-aminobutyric acid + H2O
6-aminohexanoic acid + 4-aminobutyric acid
-
low activity for EII
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
N-(6-aminohexanoyl)-8-aminooctanoic acid + H2O
6-aminohexanoate + 8-aminooctanoate
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4fold higher activity than for N-(6-aminohexanoyl)-6-aminohexanoate for enzyme EII, EII' poorly active
-
?
N-(6-aminohexanoyl)-aniline + H2O
6-aminohexanoate + aniline
-
highest activity for enzyme EII, EII' low activity
-
?
N-(8-aminooctanoyl)-6-aminohexanoic acid + H2O
8-aminooctanoic acid + 6-aminohexanoic acid
-
low activity for enzyme EII, EII' no activity
-
?
N-6-aminohexanoate hexamer + H2O
6-aminohexanoate + ?
N-6-aminohexanoate icosamer + H2O
6-aminohexanoate + ?
N-6-aminohexanoate pentamer + H2O
6-aminohexanoate + ?
N-6-aminohexanoate tetramer + H2O
6-aminohexanoate + N-6-aminohexanoate trimer
N-6-aminohexanoate trimer + H2O
6-aminohexanoate + N-(6-aminohexanoyl)-6-aminohexanoate
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
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-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
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-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
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-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
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mutant protein D181N 20fold less active, mutant D181E 200fold less active
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
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specific acitvity for EII' 0.5% that of EII
-
?
N-6-aminohexanoate hexamer + H2O
6-aminohexanoate + ?
-
-
-
?
N-6-aminohexanoate hexamer + H2O
6-aminohexanoate + ?
-
-
-
?
N-6-aminohexanoate icosamer + H2O
6-aminohexanoate + ?
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poor activity, decreasing hydrolysis with increasing polymerization number of oligomers, higher oligomers not hydrolyzed
-
?
N-6-aminohexanoate icosamer + H2O
6-aminohexanoate + ?
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poor activity, decreasing hydrolysis with increasing polymerization number of oligomers, higher oligomers not hydrolyzed
-
?
N-6-aminohexanoate pentamer + H2O
6-aminohexanoate + ?
-
-
-
?
N-6-aminohexanoate pentamer + H2O
6-aminohexanoate + ?
-
-
-
?
N-6-aminohexanoate pentamer + H2O
6-aminohexanoate + ?
-
-
-
?
N-6-aminohexanoate tetramer + H2O
6-aminohexanoate + N-6-aminohexanoate trimer
-
-
-
?
N-6-aminohexanoate tetramer + H2O
6-aminohexanoate + N-6-aminohexanoate trimer
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-
-
?
N-6-aminohexanoate tetramer + H2O
6-aminohexanoate + N-6-aminohexanoate trimer
-
-
-
?
N-6-aminohexanoate trimer + H2O
6-aminohexanoate + N-(6-aminohexanoyl)-6-aminohexanoate
-
-
-
?
N-6-aminohexanoate trimer + H2O
6-aminohexanoate + N-(6-aminohexanoyl)-6-aminohexanoate
-
-
-
?
N-6-aminohexanoate trimer + H2O
6-aminohexanoate + N-(6-aminohexanoyl)-6-aminohexanoate
-
-
-
?
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diisopropyl fluorophosphate
p-chloromercuribenzoate
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inhibition at 0.013 mM
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
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inhibition at 0.37 mM
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5.9 - 220
N-(6-aminohexanoyl)-6-aminohexanoate
6.2
N-6-aminohexanoate-trimer
-
-
5.9
N-(6-aminohexanoyl)-6-aminohexanoate
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-
15
N-(6-aminohexanoyl)-6-aminohexanoate
-
-
20
N-(6-aminohexanoyl)-6-aminohexanoate
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for EII without mutation, substitution of Asp181 to Asn or Glu affects substrate binding
80
N-(6-aminohexanoyl)-6-aminohexanoate
-
mutation D181N
220
N-(6-aminohexanoyl)-6-aminohexanoate
-
mutation D181E
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2
6-aminohexanoate trimer
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-
2.4 - 19
N-(6-aminohexanoyl)-6-aminohexanoate
2.4
N-(6-aminohexanoyl)-6-aminohexanoate
-
-
2.6
N-(6-aminohexanoyl)-6-aminohexanoate
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single mutation D181E
2.7
N-(6-aminohexanoyl)-6-aminohexanoate
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single mutation D181N
8.9
N-(6-aminohexanoyl)-6-aminohexanoate
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EII without mutation
19
N-(6-aminohexanoyl)-6-aminohexanoate
-
-
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8.5 - 9.5
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same value for enzymes EII, EII'
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Uniprot
brenda
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-
-
brenda
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nylB gene, enzyme EII
brenda
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nylB' gene, enzyme EII'
brenda
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-
-
brenda
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42000
-
2 * 42000, SDS-PAGE
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dimer
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2 * 42000, SDS-PAGE
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sitting-drop vapor-diffusion method, three-dimensional structures of the complex of 6-aminohexanoate-dimer hydrolase and 6-aminohexanoate-linear dimer and the complex of S112A-mutant of 6-aminohexanoate-dimer hydrolase and 6-aminohexanoate-linear dimer
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D181E
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mutant with increased Km and decreased activity
D181N
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mutant with increased Km and decreased activity
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50
-
EII most heat-stable
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to homogeneity, chromatography techniques, preparative gel electrophoresis
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to homogeneity, chromatography techniques, recombinant enzyme
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expression in Escherichia coli
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Kanagawa, K.; Oishi, M.; Negoro, S.; Urabe, I.; Okada, H.
Characterization of the 6-aminohexanoate-dimer hydrolase from Pseudomonas sp. NK87
J. Gen. Microbiol.
139
787-795
1993
Flavobacterium sp., Flavobacterium sp. KI72, Pseudomonas sp., Pseudomonas sp. NK87
brenda
Fujiyama, K.; Zhang, Y.Z.; Negoro, S.; Urabe, I.; Okada, H.
Characterization of hybrid enzymes between 6-aminohexanoate-dimer hydrolase and its analogues protein
J. Ferment. Bioeng.
71
298-302
1991
Flavobacterium sp., Flavobacterium sp. KI72
-
brenda
Hatanaka, H.S.; Fujiyama, K.; Negoro, S.; Urabe, I.; Okada, H.
Alteration of catalytic function of 6-aminohexanoate-dimer hydrolase by site-directed mutagenesis
J. Ferment. Bioeng.
71
191-193
1991
Flavobacterium sp., Flavobacterium sp. KI72
-
brenda
Kinoshita, S.
Microbial degradation of 6-aminohexanoic acid cyclic dimer and its enzymes
Hakko Kogaku Kaishi
60
363-375
1982
Flavobacterium sp., Flavobacterium sp. KI72
-
brenda
Kinoshita, S.; Terada, T.; Taniguchi, T.; Takene, Y.; Masuda, S.
Purification and characterization of 6-aminohexanoic acid-oligomer hydrolase of Flavobacterium sp. KI72
Eur. J. Biochem.
116
547-551
1981
Flavobacterium sp., Flavobacterium sp. KI72
brenda
Negoro, S.; Ohki, T.; Shibata, N.; Sasa, K.; Hayashi, H.; Nakano, H.; Yasuhira, K.; Kato, D.; Takeo, M.; Higuchi, Y.
Nylon-oligomer degrading enzyme/substrate complex: catalytic mechanism of 6-aminohexanoate-dimer hydrolase
J. Mol. Biol.
370
142-156
2007
Flavobacterium sp. (P07062)
brenda