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4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenylbutyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
6-aminohexanoate cyclic-oligomer + H2O
?
6-aminohexanoate dimer + H2O
2 6-aminohexanoate
N-(4-aminobutyryl)-4-aminobutyric acid + H2O
4-aminobutyric acid + 4-aminobutyric acid
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
N-(6-aminohexanoyl)-4-aminobutyric acid + H2O
6-aminohexanoic acid + 4-aminobutyric acid
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
N-(6-aminohexanoyl)-8-aminooctanoic acid + H2O
6-aminohexanoate + 8-aminooctanoate
N-(6-aminohexanoyl)-aniline + H2O
6-aminohexanoate + aniline
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
additional information
?
-
6-aminohexanoate cyclic-oligomer + H2O
?
-
-
-
-
?
6-aminohexanoate cyclic-oligomer + H2O
?
-
-
-
-
?
6-aminohexanoate cyclic-oligomer + H2O
?
-
-
-
-
?
6-aminohexanoate cyclic-oligomer + H2O
?
-
-
-
-
?
6-aminohexanoate cyclic-oligomer + H2O
?
-
-
-
-
?
6-aminohexanoate dimer + H2O
2 6-aminohexanoate
-
-
-
?
6-aminohexanoate dimer + H2O
2 6-aminohexanoate
the enzyme hydrolyzes the Ahx oligomers by an exo-type mechanism
-
-
?
N-(4-aminobutyryl)-4-aminobutyric acid + H2O
4-aminobutyric acid + 4-aminobutyric acid
-
very low activity for EII
-
?
N-(4-aminobutyryl)-4-aminobutyric acid + H2O
4-aminobutyric acid + 4-aminobutyric acid
-
very low activity for EII
-
?
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
-
-
-
-
?
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
-
-
-
-
?
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
-
-
-
-
?
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
-
-
-
-
?
N-(6-aminohexanoyl)-4-aminobutyric acid + H2O
6-aminohexanoic acid + 4-aminobutyric acid
-
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
2 6-aminohexanoate
-
-
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
-
the enzyme is involved degradation of nylon-6
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
-
-
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
-
the enzyme is involved degradation of nylon-6
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
-
-
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
-
the enzyme is involved degradation of nylon-6
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
-
-
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
-
the enzyme is involved degradation of nylon-6
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate
-
the enzyme is responsible for the degradation of nylon-6 industrial production by-products
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate
-
isozyme EII' shows only about 0.5% of the activity of EII
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate
-
the enzyme hydrolyzes the linear dimer substrate
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
-
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
-
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
-
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
-
mutant protein D181N 20fold less active, mutant D181E 200fold less active
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
-
specific acitvity for EII' 0.5% that of EII
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
-
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
-
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
-
specific acitvity for EII' 0.5% that of EII
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
-
mutant protein D181N 20fold less active, mutant D181E 200fold less active
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
-
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
-
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
-
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
-
-
-
?
N-(6-aminohexanoyl)-8-aminooctanoic acid + H2O
6-aminohexanoate + 8-aminooctanoate
-
4fold higher activity than for N-(6-aminohexanoyl)-6-aminohexanoate for enzyme EII, EII' poorly active
-
?
N-(6-aminohexanoyl)-8-aminooctanoic acid + H2O
6-aminohexanoate + 8-aminooctanoate
-
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-(6-aminohexanoyl)-aniline + H2O
6-aminohexanoate + aniline
-
highest activity for enzyme EII, EII' low activity
-
?
N-6-aminohexanoate hexamer + H2O
6-aminohexanoate + ?
-
-
-
?
N-6-aminohexanoate hexamer + H2O
6-aminohexanoate + ?
-
-
-
?
N-6-aminohexanoate hexamer + H2O
6-aminohexanoate + ?
-
-
-
?
N-6-aminohexanoate hexamer + H2O
6-aminohexanoate + ?
-
-
-
?
N-6-aminohexanoate hexamer + H2O
6-aminohexanoate + ?
-
-
-
?
N-6-aminohexanoate icosamer + H2O
6-aminohexanoate + ?
-
poor activity, decreasing hydrolysis with increasing polymerization number of oligomers, higher oligomers not hydrolyzed
-
?
N-6-aminohexanoate icosamer + H2O
6-aminohexanoate + ?
-
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 pentamer + H2O
6-aminohexanoate + ?
-
-
-
?
N-6-aminohexanoate pentamer + H2O
6-aminohexanoate + ?
-
-
-
?
N-6-aminohexanoate pentamer + H2O
6-aminohexanoate + ?
-
-
-
?
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
-
-
-
?
N-6-aminohexanoate tetramer + H2O
6-aminohexanoate + N-6-aminohexanoate trimer
-
-
-
?
N-6-aminohexanoate tetramer + H2O
6-aminohexanoate + N-6-aminohexanoate trimer
-
-
-
?
N-6-aminohexanoate tetramer + H2O
6-aminohexanoate + N-6-aminohexanoate trimer
-
-
-
?
N-6-aminohexanoate tetramer + H2O
6-aminohexanoate + N-6-aminohexanoate trimer
-
-
-
?
N-6-aminohexanoate tetramer + H2O
6-aminohexanoate + N-6-aminohexanoate trimer
-
-
-
?
N-6-aminohexanoate tetramer + H2O
6-aminohexanoate + N-6-aminohexanoate trimer
-
highest relative activity
major products, the trimer is subsequently subjected to hydrolysis, digests exogenously linear oligomers from the N-terminus as monomeric units
?
N-6-aminohexanoate tetramer + H2O
6-aminohexanoate + N-6-aminohexanoate trimer
-
highest relative activity
major products, the trimer is subsequently subjected to hydrolysis, digests exogenously linear oligomers from the N-terminus as monomeric units
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
additional information
?
-
-
substrate specificity of EII and mutant Hyb24, no activity with D-Ala-D-Ala
-
-
?
additional information
?
-
enzyme 6-aminohexanoate-dimer hydrolase catalyzes amide synthesis. The yield of this reverse reaction in 90% t-butyl alcohol varies drastically when enzyme mutants with substitutions of several amino acids located at the entrance of the catalytic cleft are used. The shift of the internal equilibrium between the enzyme-substrate complex and enzyme-product complex by the water-excluding effect alters the rate of the forward and reverse reactions. The local hydrophobic environment potentially provides a reaction center suitable for efficient amide synthesis
-
-
?
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A61V/A253T/F264C/D370Y
-
site-directed mutagenesis, 10fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate
D181E
-
site-directed mutagenesis of EII, the mutant shows reduced activity compared to the wild-type enzyme
D181H
-
site-directed mutagenesis of EII, the mutant shows highly reduced activity compared to the wild-type enzyme
D181K
-
site-directed mutagenesis of EII, nearly inactive mutant
D181N
-
site-directed mutagenesis of EII, the mutant shows reduced activity compared to the wild-type enzyme
T3A/P4R/T5S/S8Q/D15G/D370Y
-
site-directed mutagenesis, mutant Hyb24, by five amino acid replacement in EII' for residues of EII, plus 2 additional exchanges for EII residues leading to a 10fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate
T3A/P4R/T5S/S8Q/D15G/G181D
-
site-directed mutagenesis, mutant Hyb24, by five amino acid replacement in EII' for residues of EII, plus 2 additional exchanges for EII residues leading to a 10fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate
T3A/P4R/T5S/S8Q/D15G/G181D/D370Y
-
site-directed mutagenesis, mutant Hyb24, by five amino acid replacement in EII' for residues of EII, plus 2 additional exchanges for EII residues leading to a 100fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate
D181E
-
mutant with increased Km and decreased activity
D181N
-
mutant with increased Km and decreased activity
D181E
-
mutant with increased Km and decreased activity
-
D181N
-
mutant with increased Km and decreased activity
-
A61V/A124V/R187S/F264C/G291R/G338A/D370Y
site-directed mutagenesis
G181D/H266N
construction of NylB mutant enzyme Hyb-24DN, the activity in Hyb-24 is enhanced 150fold by the two substitutions, where Asp181-COO- stabilizes the substrate binding by electrostatic interactions with Ald-NH3+, and Asn266 cooperatively improves the electrostatic environment with Asp181
R187A
site-directed mutagenesis, the substitution in the parental Hyb-24DNY decreases the specific activity (initial reaction rate) of synthesis to 37% of the level of Hyb-24DNY
R187G
site-directed mutagenesis, the substitution in the parental Hyb-24DNY decreases the specific activity (initial reaction rate) of synthesis to 15% of the level of Hyb-24DNY
R187S
site-directed mutagenesis, the substitution in the parental Hyb-24DNY decreases the specific activity (initial reaction rate) of synthesis to 24% of the level of Hyb-24DNY
R187S/F264C/D370Y
site-directed mutagenesis, the substitutions also enhance the Ald-hydrolytic activity 80fold over the parental Hyb-24 enzyme. The directly evolved enzyme (Hyb-S4M94) possesses almost no Ald-synthetic activity, although it possesses high levels of the hydrolytic activity even in 90% t-butyl alcohol. In this mutant enzyme, the R187S/F264C substitutions stabilizes the binding at the N-terminal region of Ald, while D370Y substitution stabilizes the binding at the C-terminal region of Ald
additional information
construction of chimeric NylB/NylB' mutants Hyb-24DN and Hyb-24DNY. A NylB/NylB' hybrid enzyme Hyb-24 (NylB' containing T3A-P4R-T5S-S8Q-D15G substitutions) has about 0.5% of the NylB level of Ald-hydrolytic activity. Surface structure of the entrance of the catalytic cleft of the Hyb-24DNY and its mutant enzymes, wild-type and mutant kinetics, detailed overview
T3A/P4R/T5S/S8Q/D15G
-
construction of a hybrid of isozymes EII and EII', termed Hyb24, by five amino acid replacement in EII', the mutant shows the same activity as EII'
T3A/P4R/T5S/S8Q/D15G
-
site-directed mutagenesis, construction of a hybrid of isozymes EII and EII', termed Hyb24, by five amino acid replacement in EII', the mutant shows the same activity as EII'
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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., Pseudomonas sp., Flavobacterium sp. KI72, 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
Ohki, T.; Mizuno, N.; Shibata, N.; Takeo, M.; Negoro, S.; Higuchi, Y.
Crystallization and X-ray diffraction analysis of 6-aminohexanoate-dimer hydrolase from Arthrobacter sp. KI72
Acta Crystallogr. Sect. F
61
928-930
2005
Arthrobacter sp.
brenda
Ohki, T.; Wakitani, Y.; Takeo, M.; Yasuhira, K.; Shibata, N.; Higuchi, Y.; Negoro, S.
Mutational analysis of 6-aminohexanoate-dimer hydrolase: relationship between nylon oligomer hydrolytic and esterolytic activities
FEBS Lett.
580
5054-5058
2006
Arthrobacter sp.
brenda
Negoro, S.; Ohki, T.; Shibata, N.; Mizuno, N.; Wakitani, Y.; Tsurukame, J.; Matsumoto, K.; Kawamoto, I.; Takeo, M.; Higuchi, Y.
X-ray crystallographic analysis of 6-aminohexanoate-dimer hydrolase: molecular basis for the birth of a nylon oligomer-degrading enzyme
J. Biol. Chem.
280
39644-39652
2005
Arthrobacter sp.
brenda
Yasuhira, K.; Tanaka, Y.; Shibata, H.; Kawashima, Y.; Ohara, A.; Kato, D.; Takeo, M.; Negoro, S.
6-Aminohexanoate oligomer hydrolases from the alkalophilic bacteria Agromyces sp. strain KY5R and Kocuria sp. strain KY2
Appl. Environ. Microbiol.
73
7099-7102
2007
Arthrobacter sp., Agromyces sp., Kocuria sp., Kocuria sp. KY2, Agromyces sp. KY5R
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
Taguchi, H.; Wakamatsu, M.; Aso, K.; Ono, S.; Shin, T.; Akamatsu, T.
A simple assay for 6-aminohexanoate-oligomer-hydrolase using N-(4-nitrophenyl)-6-aminohexanamide
J. Biosci. Bioeng.
114
586-588
2012
Arthrobacter sp., Pseudomonas sp., Pseudomonas sp. NK87, Arthrobacter sp. KI72
brenda
akehara, I.; Fujii, T.; Tanimoto, Y.; Kato, D.I.; Takeo, M.; Negoro, S.
Metabolic pathway of 6-aminohexanoate in the nylon oligomer-degrading bacterium Arthrobacter sp. KI72 identification of the enzymes responsible for the conversion of 6-aminohexanoate to adipate
Appl. Microbiol. Biotechnol.
102
801-814
2018
Paenarthrobacter ureafaciens (P07061)
brenda
Negoro, S.; Kawashima, Y.; Shibata, N.; Kobayashi, T.; Baba, T.; Lee, Y.H.; Kamiya, K.; Shigeta, Y.; Nagai, K.; Takehara, I.; Kato, D.; Takeo, M.; Higuchi, Y.
Mutations affecting the internal equilibrium of the reaction catalyzed by 6-aminohexanoate-dimer hydrolase
FEBS Lett.
590
3133-3143
2016
Paenarthrobacter ureafaciens (P07061)
brenda
Ando, H.; Shigeta, Y.; Baba, T.; Watanabe, C.; Okiyama, Y.; Mochizuki, Y.; Nakano, M.
Hydration effects on enzyme-substrate complex of nylon oligomer hydrolase inter-fragment interaction energy study by the fragment molecular orbital method
Mol. Phys.
113
319-326
2015
Paenarthrobacter ureafaciens (P07061)
-
brenda