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
nylon-6 oligomer degradation
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Caprolactam degradation
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Microbial metabolism in diverse environments
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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
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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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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-
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?
4-nitrophenylbutyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
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-
-
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?
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
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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
UNIPROT
ORGANISM
Flavobacterium sp. (strain K172);
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, 2.0–2.2 M ammonium sulfate, 0.1–0.2 M lithium sulfate, at 10°C, 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, 10°C, 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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