Information on EC 3.5.1.117 - 6-aminohexanoate-oligomer endohydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.1.117
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RECOMMENDED NAME
GeneOntology No.
6-aminohexanoate-oligomer endohydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Caprolactam degradation
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Microbial metabolism in diverse environments
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nylon-6 oligomer degradation
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SYSTEMATIC NAME
IUBMB Comments
6-aminohexanoate oligomer endoamidohydrolase
The enzyme is involved in degradation of nylon-6 oligomers. It degrades linear or cyclic oligomers of poly(6-aminohexanoate) with a degree of polymerization greater than three (n > 3) by endo-type cleavage, to oligomers of a length of two or more (2 <= x < n). It shows negligible activity with N-(6-aminohexanoyl)-6-aminohexanoate (cf. EC 3.5.1.46, 6-aminohexanoate-oligomer exo hydrolase) or with 1,8-diazacyclotetradecane-2,9-dione (cf. EC 3.5.2.12, 6-aminohexanoate-cyclic-dimer hydrolase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6-aminohexanoate cyclic oligomer + H2O
6-aminohexanoate
show the reaction diagram
6-aminohexanoate cyclic oligomer + H2O
?
show the reaction diagram
H2N(CH2)3CO-NH(CH2)5COOH + H2O
?
show the reaction diagram
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4% activity compared to H2N(CH2)5CO-NH(CH2)5COOH
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?
H2N(CH2)5CO-NH(CH2)3COOH + H2O
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show the reaction diagram
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15% activity compared to H2N(CH2)5CO-NH(CH2)5COOH
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?
H2N(CH2)5CO-NH(CH2)5COOH + H2O
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show the reaction diagram
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100% activity
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?
H2N(CH2)5CO-NH(CH2)7COOH + H2O
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show the reaction diagram
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600% activity compared to H2N(CH2)5CO-NH(CH2)5COOH
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?
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
show the reaction diagram
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
show the reaction diagram
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
show the reaction diagram
endo-type reaction
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?
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
show the reaction diagram
endo-type reaction
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?
N-(6-aminohexanoyl)n-6-aminohexanoate + H2O
N-(6-aminohexanoyl)n-x + N-(6-aminohexanoyl)x-6-aminohexanoate
show the reaction diagram
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?
nylon oligomer + H2O
?
show the reaction diagram
nylon-6 + H2O
?
show the reaction diagram
nylon-6 polymer + H2O
?
show the reaction diagram
nylon-66 polymer + H2O
?
show the reaction diagram
[N-(6-aminohexanoyl)]n + H2O
[N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nylon-6 polymer + H2O
?
show the reaction diagram
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nylon-6 is the preferred nyloln substrate
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?
nylon-66 polymer + H2O
?
show the reaction diagram
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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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?
[N-(6-aminohexanoyl)]n + H2O
[N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
show the reaction diagram
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 2
N-(4-nitrophenyl)-6-aminohexanamide
0.6 - 15
N-(6-aminohexanoyl)-6-aminohexanoate
additional information
6-aminohexanoate cyclic oligomer
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.5
6-aminohexanoate cyclic oligomer
Agromyces sp.
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pH 7.3, 60°C, mutant enzyme D122G/H130Y/D36A/E236Q
21
N-(4-nitrophenyl)-6-aminohexanamide
Pseudomonas sp.
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pH and temperature not specified in the publication
9.2 - 19
N-(6-aminohexanoyl)-6-aminohexanoate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.3
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pH 7.2, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9513
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x * 27408 + x * 9513, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, calculation from nucleotide sequence
27408
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x * 27408 + x * 9513, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, calculation from nucleotide sequence
31000
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x * 31000 + x * 9000, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
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1 * 27000 + 1 * 9000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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sitting drop vapor diffusion method, using sodium citrate as a precipitant in 0.1 M HEPES buffer pH 7.5 containing 0.2 M NaCl
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sitting drop vapor diffusion method, with ammonium sulfate as a precipitant in 0.1 M HEPES buffer pH 7.5 containing 0.2 M NaCl and 25% (v/v) glycerol
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41
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melting temperature of of mutant enzyme L137A
43
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melting temperature of of mutant enzyme G111S
51
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melting temperature of mutant enzyme G111S/D122G/H130Y/L137A
52
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melting temperature of wild type enzyme
54
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melting temperature of mutant enzyme D122G/H130Y/L137A
55
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30 min, enzyme retains 90% of its activity
63
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melting temperature of mutant enzyme H130Y; melting temperature of of mutant enzyme H130Y
70
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30 min, more than 90% of enzyme activity of mutant D122G/H130Y/D36A/E263Q is retained
76
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melting temperature of mutant enzyme D122G; melting temperature of of mutant enzyme D122G
78
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melting temperature of mutant enzyme G111S/D122G/H130Y
81
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melting temperature of of mutant enzyme D122G/H130Y
83
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melting temperature of mutant enzyme D122G/H130Y/V225M
84
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melting temperature of mutant enzyme D122G/H130Y/D36A or D122G/H130Y/E263Q
88
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melting temperature of mutant D122G/H130Y/D36A/E263Q
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Q Sepharose column chromatography, Sephacryl S-200 and gel filtration
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ammonium sulfate precipitation, Q Sepharose column chromatography, Sephacryl S-200 gel filtration
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recombinant quadruple mutant from Escherichia colistraiin JM109 by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 cells
expression in Escherichia coli
gene nylCp2, recombinant expression of enzyme quadruple mutant in Escherichia coli straiin JM109
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D122G
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mutation increases the melting temperature by 24°C compared to wild-type enzyme
D122G/H130Y
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mutation increases the melting temperature by 29°C compared to wild-type enzyme
D122G/H130Y/D36A
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mutation increases the melting temperature by 32°C compared to wild-type enzyme
D122G/H130Y/D36A/E236Q
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mutation increases the melting temperature by 36°C compared to wild-type enzyme
D122G/H130Y/D36A/E263Q
D122G/H130Y/E263Q
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mutation increases the melting temperature by 32°C compared to wild-type enzyme
D122G/H130Y/L137A
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mutation increases the melting temperature by 2°C compared to wild-type enzyme
G111S
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mutation decreases the melting temperature by 9°C compared to wild-type enzyme
G111S/D122G/H130Y
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mutation increases the melting temperature by 26°C compared to wild-type enzyme
G111S/D122G/H130Y/L137A
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mutation decreases the melting temperature by 1°C compared to wild-type enzyme
H130Y
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mutation increases the melting temperature by 11°C compared to wild-type enzyme
L137A
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mutation decreases the melting temperature by 11°C compared to wild-type enzyme
D122G
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mutation increases the melting temperature by 24°C compared to wild-type enzyme
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D122G/H130Y/D36A/E263Q
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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
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G111S
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mutation decreases the melting temperature by 9°C compared to wild-type enzyme
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H130Y
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mutation increases the melting temperature by 11°C compared to wild-type enzyme
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L137A
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mutation decreases the melting temperature by 11°C compared to wild-type enzyme
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D15G
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site-directed mutagenesis
D181G
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site-directed mutagenesis
G181D/H266N
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site-directed mutagenesis
G181D/H266N/D370Y
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site-directed mutagenesis
P4R
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site-directed mutagenesis
S8Q
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site-directed mutagenesis
T3A
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site-directed mutagenesis
T5S
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site-directed mutagenesis
Y170F
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site-directed mutagenesis, the Tyr170 is replaced by phenylalanine, which is unable to form a hydrogen bond with the amide bond, thus, resulting in an increase in the activation barrier of more than 10 kcal/mol, but despite the lack of hydrogen bonding between the Y170F and the substrate, the highest free energy barrier for the induced-fit is similar to that of wild-type suggesting that in the induced-fit process, kinetics is little affected by the mutation, hybrid quantum mechanics/molecular mechanics (QM/MM) dynamical simulations
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry