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Information on EC 3.5.1.46 - 6-aminohexanoate-oligomer exohydrolase
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3.5.1.46 6-aminohexanoate-oligomer exohydrolaseIUBMB 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.
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Word Map
- 3.5.1.46
- flavobacterium
- arthrobacter
- nylon-6
- amide
- beta-lactamase
- carboxylesterase
- esterase
-
esterolytic
- hydrolases
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vapour-diffusion
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tetrahedral
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penicillin-recognizing
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man-made
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sitting-drop
-
compendium
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
6-aminohexanoate-dimer hydrolase, hyb-24, nylon oligomer hydrolase, 6-aminohexanoate dimer hydrolase, 6-aminohexanoate oligomer hydrolase, nylcp2, hyb-24dn, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-aminohexanoate oligomer hydrolase
6-aminohexanoate-dimer hydrolase
6-aminohexanoic acid oligomer hydrolase
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-
-
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EII
EII'
N-(6-aminohexanoyl)-6-aminohexanoate amidohydrolase
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NylB
NylCA
NylCK
nylon oligomer hydrolase
Nylon oligomers degrading enzyme EII
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-
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Nylon oligomers degrading enzyme EII'
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-
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6-aminohexanoate-dimer hydrolase
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-1 + 6-aminohexanoate
(1)
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-
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N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate
structure-function relationship
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N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate
Also hydrolyses oligomers of 6-aminohexanoate containing up to six residues, but more slowly
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N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate
the residues are removed sequentially from the N-terminus
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N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate
Ser112 is a nucleophilic catalytic residue, Asp181 and Asn226 are also required
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N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate
structure-function relationship, residues 370 and 181 are imporatant for enzyme activity
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N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate
(2)
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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CAS REGISTRY NUMBER
COMMENTARY
75216-15-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-(8-aminooctanoyl)-6-aminohexanoic acid + H2O
8-aminooctanoic acid + 6-aminohexanoic acid
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low activity for enzyme EII, EII' no activity
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?
6-aminohexanoate dimer + H2O
2 6-aminohexanoate
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-
-
?
6-aminohexanoate dimer + H2O
2 6-aminohexanoate
the enzyme hydrolyzes the Ahx oligomers by an exo-type mechanism
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-
?
N-(4-aminobutyryl)-4-aminobutyric acid + H2O
4-aminobutyric acid + 4-aminobutyric acid
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very low activity for EII
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?
N-(4-aminobutyryl)-4-aminobutyric acid + H2O
4-aminobutyric acid + 4-aminobutyric acid
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very low activity for EII
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?
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
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-
-
-
?
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
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-
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-
?
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
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?
N-(4-nitrophenyl)-6-aminohexanamide + H2O
4-nitroaniline + 6-aminohexanoate
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-
-
?
N-(6-aminohexanoyl)-4-aminobutyric acid + H2O
6-aminohexanoic acid + 4-aminobutyric acid
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low activity for EII
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?
N-(6-aminohexanoyl)-4-aminobutyric acid + H2O
6-aminohexanoic acid + 4-aminobutyric acid
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low activity for EII
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?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
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the enzyme is involved degradation of nylon-6
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-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
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-
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
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the enzyme is involved degradation of nylon-6
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-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
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the enzyme is involved degradation of nylon-6
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?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
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the enzyme is involved degradation of nylon-6
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?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate
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the enzyme is responsible for the degradation of nylon-6 industrial production by-products
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?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate
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isozyme EII' shows only about 0.5% of the activity of EII
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?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate
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the enzyme hydrolyzes the linear dimer substrate
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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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?
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
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?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
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specific acitvity for EII' 0.5% that of EII
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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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specific acitvity for EII' 0.5% that of EII
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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
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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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?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate + 6-aminohexanoate
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-
-
?
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
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?
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
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?
N-(6-aminohexanoyl)-aniline + H2O
6-aminohexanoate + aniline
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highest activity for enzyme EII, EII' low activity
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?
N-(6-aminohexanoyl)-aniline + H2O
6-aminohexanoate + aniline
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highest activity for enzyme EII, EII' low activity
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?
N-6-aminohexanoate hexamer + H2O
6-aminohexanoate + ?
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?
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
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?
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
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?
N-6-aminohexanoate pentamer + H2O
6-aminohexanoate + ?
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?
N-6-aminohexanoate pentamer + H2O
6-aminohexanoate + ?
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?
N-6-aminohexanoate pentamer + H2O
6-aminohexanoate + ?
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?
N-6-aminohexanoate pentamer + H2O
6-aminohexanoate + ?
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?
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
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?
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
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?
N-6-aminohexanoate tetramer + H2O
6-aminohexanoate + N-6-aminohexanoate trimer
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-
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?
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
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?
N-6-aminohexanoate tetramer + H2O
6-aminohexanoate + N-6-aminohexanoate trimer
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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
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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
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?
N-6-aminohexanoate trimer + H2O
6-aminohexanoate + N-(6-aminohexanoyl)-6-aminohexanoate
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-
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?
N-6-aminohexanoate trimer + H2O
6-aminohexanoate + N-(6-aminohexanoyl)-6-aminohexanoate
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-
-
?
N-6-aminohexanoate trimer + H2O
6-aminohexanoate + N-(6-aminohexanoyl)-6-aminohexanoate
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-
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?
N-6-aminohexanoate trimer + H2O
6-aminohexanoate + N-(6-aminohexanoyl)-6-aminohexanoate
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-
-
?
N-6-aminohexanoate trimer + H2O
6-aminohexanoate + N-(6-aminohexanoyl)-6-aminohexanoate
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-
-
?
N-6-aminohexanoate trimer + H2O
6-aminohexanoate + N-(6-aminohexanoyl)-6-aminohexanoate
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-
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?
N-6-aminohexanoate trimer + H2O
6-aminohexanoate + N-(6-aminohexanoyl)-6-aminohexanoate
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-
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?
N-6-aminohexanoate trimer + H2O
6-aminohexanoate + N-(6-aminohexanoyl)-6-aminohexanoate
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-
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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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-
?
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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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
6-aminohexanoate
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the enzyme is responsible for the degradation of nylon-6 industrial production by-products
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-
?
6-aminohexanoate dimer + H2O
2 6-aminohexanoate
the enzyme hydrolyzes the Ahx oligomers by an exo-type mechanism
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-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
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the enzyme is involved degradation of nylon-6
-
-
?
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
-
the enzyme is involved degradation of nylon-6
-
-
?
N-(6-aminohexanoyl)-6-aminohexanoate + H2O
2 6-aminohexanoate
-
the enzyme is involved degradation of nylon-6
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.9
6-aminohexanoate dimer
pH 7.3, 30°C, recombinant Hyb-24DNY mutant R187A, hydrolysis in 90% t-butyl alcohol
2.1
6-aminohexanoate dimer
pH 7.3, 30°C, recombinant enzyme Hyb-24DNY, hydrolysis in 90% t-butyl alcohol
2.2
6-aminohexanoate dimer
pH 7.3, 30°C, recombinant Hyb-24DNY mutant R187S, hydrolysis in 90% t-butyl alcohol
2.6
6-aminohexanoate dimer
pH 7.3, 30°C, recombinant Hyb-24DNY mutant R187G, hydrolysis in 90% t-butyl alcohol
20
N-(6-aminohexanoyl)-6-aminohexanoate
-
for EII without mutation, substitution of Asp181 to Asn or Glu affects substrate binding
additional information
additional information
-
Km for 6-aminohexanoate cyclic-oligomer: 0.44 mg/ml
-
additional information
additional information
-
Km for 6-aminohexanoate cyclic-oligomer: 0.49 mg/ml
-
additional information
additional information
-
Km for 6-aminohexanoate cyclic-oligomer: 3.7 mg/ml
-
additional information
additional information
Michaelis-Menten kinetics, kinetic study of wild-type and mutant enzymes
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.29
6-aminohexanoate dimer
pH 7.3, 30°C, recombinant Hyb-24DNY mutant R187A, hydrolysis in 90% t-butyl alcohol
0.63
6-aminohexanoate dimer
pH 7.3, 30°C, recombinant Hyb-24DNY mutant R187S, hydrolysis in 90% t-butyl alcohol
0.91
6-aminohexanoate dimer
pH 7.3, 30°C, recombinant Hyb-24DNY mutant R187G, hydrolysis in 90% t-butyl alcohol
1.17
6-aminohexanoate dimer
pH 7.3, 30°C, recombinant enzyme Hyb-24DNY, hydrolysis in 90% t-butyl alcohol
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.153
6-aminohexanoate dimer
pH 7.3, 30°C, recombinant Hyb-24DNY mutant R187A, hydrolysis in 90% t-butyl alcohol
0.286
6-aminohexanoate dimer
pH 7.3, 30°C, recombinant Hyb-24DNY mutant R187S, hydrolysis in 90% t-butyl alcohol
0.35
6-aminohexanoate dimer
pH 7.3, 30°C, recombinant Hyb-24DNY mutant R187G, hydrolysis in 90% t-butyl alcohol
0.557
6-aminohexanoate dimer
pH 7.3, 30°C, recombinant enzyme Hyb-24DNY, hydrolysis in 90% t-butyl alcohol
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Flavobacterium sp. K172
UniProt
brenda
formerly Flavobacterium sp., strain K172, enzyme form EII and cryptic enzyme form EII'
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-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE