Information on EC 3.5.1.46 - 6-aminohexanoate-oligomer exohydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.1.46
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RECOMMENDED NAME
GeneOntology No.
6-aminohexanoate-oligomer exohydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate
show the reaction diagram
[N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-1 + 6-aminohexanoate
show the reaction diagram
(1)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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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
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.
CAS REGISTRY NUMBER
COMMENTARY hide
75216-15-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain KY5R
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Manually annotated by BRENDA team
strain KY5R
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Manually annotated by BRENDA team
strain KY2
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Manually annotated by BRENDA team
strain KY2
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
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-
-
-
?
4-nitrophenylbutyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
6-aminohexanoate cyclic-oligomer + H2O
?
show the reaction diagram
N-(4-aminobutyryl)-4-aminobutyric acid + H2O
4-aminobutyric acid + 4-aminobutyric acid
show the reaction diagram
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
show the reaction diagram
N-(6-aminohexanoyl)-4-aminobutyric acid + H2O
6-aminohexanoic acid + 4-aminobutyric acid
show the reaction diagram
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
show the reaction diagram
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate
show the reaction diagram
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
show the reaction diagram
N-(6-aminohexanoyl)-8-aminooctanoic acid + H2O
6-aminohexanoate + 8-aminooctanoate
show the reaction diagram
N-(6-aminohexanoyl)-aniline + H2O
6-aminohexanoate + aniline
show the reaction diagram
N-(8-aminooctanoyl)-6-aminohexanoic acid + H2O
8-aminooctanoic acid + 6-aminohexanoic acid
show the reaction diagram
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low activity for enzyme EII, EII' no activity
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?
N-6-aminohexanoate hexamer + H2O
6-aminohexanoate + ?
show the reaction diagram
N-6-aminohexanoate icosamer + H2O
6-aminohexanoate + ?
show the reaction diagram
N-6-aminohexanoate pentamer + H2O
6-aminohexanoate + ?
show the reaction diagram
N-6-aminohexanoate tetramer + H2O
6-aminohexanoate + N-6-aminohexanoate trimer
show the reaction diagram
N-6-aminohexanoate trimer + H2O
6-aminohexanoate + N-(6-aminohexanoyl)-6-aminohexanoate
show the reaction diagram
nylon-6 + H2O
?
show the reaction diagram
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?
additional information
?
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substrate specificity of EII and mutant Hyb24, no activity with D-Ala-D-Ala
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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
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
show the reaction diagram
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate
show the reaction diagram
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the enzyme is responsible for the degradation of nylon-6 industrial production by-products
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?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diisopropyl fluorophosphate
p-chloromercuribenzoate
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inhibition at 0.013 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 2
N-(4-nitrophenyl)-6-aminohexanamide
0.6 - 220
N-(6-aminohexanoyl)-6-aminohexanoate
6.2
N-6-aminohexanoate-trimer
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additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
6-aminohexanoate trimer
Flavobacterium sp.
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2.4 - 19
N-(6-aminohexanoyl)-6-aminohexanoate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.7
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purified from parental strain
4
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purified from cloned Escherichia coli strain
4.16
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purified recombinant wild-type EII
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 9.5
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same value for enzymes EII, EII'
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
76000
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gel filtration
84000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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analysis of domain structures of EII, cryptic enzyme form EII', and EII-EII'-hybrid Hyb24
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant Hyb24 by sitting drop vapor diffusion from 0.1 M MES, pH 6.5, 2.02.2 M ammonium sulfate, 0.10.2 M lithium sulfate, at 10C, 2 ml of sample mixed with 2 ml of reservoir solution, preparation of HgCl2 heavy atom derivatives, X-ray diffraction structure determination and analysis at 1.8 A resolution
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purified recombinant Hyb24, sitting drop vapor diffusion, 38 mg/ml protein in 20 mM phosphate, pH 7.3, and 10% glycerol, 0.02 ml of protein solution is mixed with the same volume of reservoir solution and equilibrated against 0.8 ml of reservoir solution, 10C, 48 h, preparation of methylmercuric chloride heavy atom derivatives, X-ray diffraction structure determination and analysis at 1.75-1.8 A resolution
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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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
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172042
6.8 - 8.5
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stable within
172039
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
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stable for 1 h
40
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30 min, stable up to
45
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stable up to
50
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EII most heat-stable
55
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30 min, enzyme retains 90% of its activity
60
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30 min, enzyme retains 90% of its activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged EII from Escherichia coli strain by nickel affinity chromatography, recombinant EII-EII'-hybrid Hyb24 from Escherichia coli strain KP3998 by anion exchange chromatography, gel filtration, and again anion exchange chromatography, both enzymes to homogeneity
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recombinant His-tagged EII-EII'-hybrid Hyb24 from Escherichia coli strain KP3998 by anion exchange chromatography, gel filtration, and again anion exchange chromatography, to homogeneity
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to homogeneity, chromatography techniques, preparative gel electrophoresis
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to homogeneity, chromatography techniques, recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of the His-tagged EII and the EII-EII'-hybrid Hyb24 in Escherichia coli strains JM109 and KP3998, respectively
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nylB24 gene, expression of the His-tagged EII-EII'-hybrid Hyb24 in Escherichia coli strain KP3998
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A61V/A253T/F264C/D370Y
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site-directed mutagenesis, 10fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate
D181E
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site-directed mutagenesis of EII, the mutant shows reduced activity compared to the wild-type enzyme
D181H
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site-directed mutagenesis of EII, the mutant shows highly reduced activity compared to the wild-type enzyme
D181K
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site-directed mutagenesis of EII, nearly inactive mutant
D181N
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site-directed mutagenesis of EII, the mutant shows reduced activity compared to the wild-type enzyme
T3A/P4R/T5S/S8Q/D15G
T3A/P4R/T5S/S8Q/D15G/D370Y
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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
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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
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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
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mutant with increased Km and decreased activity
D181N
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mutant with increased Km and decreased activity
D181E
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mutant with increased Km and decreased activity
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D181N
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mutant with increased Km and decreased activity
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