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Information on EC 3.5.1.46 - 6-aminohexanoate-oligomer exohydrolase and Organism(s) Flavobacterium sp. and UniProt Accession P07062

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IUBMB 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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Flavobacterium sp.
UNIPROT: P07062
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The taxonomic range for the selected organisms is: Flavobacterium sp.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
6-aminohexanoate-dimer hydrolase, hyb-24, nylon oligomer hydrolase, 6-aminohexanoate dimer hydrolase, nylcp2, hyb-24dn, 6-aminohexanoate oligomer hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nylon-oligomer degrading enzyme
-
6-aminohexanoate-dimer hydrolase
-
-
-
-
6-aminohexanoic acid oligomer hydrolase
-
-
-
-
N-(6-aminohexanoyl)-6-aminohexanoate amidohydrolase
-
-
-
-
Nylon oligomers degrading enzyme EII
-
-
-
-
Nylon oligomers degrading enzyme EII'
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
nylon-6 + H2O
?
show the reaction diagram
-
-
-
?
N-(4-aminobutyryl)-4-aminobutyric acid + H2O
4-aminobutyric acid + 4-aminobutyric acid
show the reaction diagram
-
very low activity for EII
-
?
N-(6-aminohexanoyl)-4-aminobutyric acid + H2O
6-aminohexanoic acid + 4-aminobutyric acid
show the reaction diagram
-
low activity for EII
-
?
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
-
4fold higher activity than for N-(6-aminohexanoyl)-6-aminohexanoate for enzyme EII, EII' poorly active
-
?
N-(6-aminohexanoyl)-aniline + H2O
6-aminohexanoate + aniline
show the reaction diagram
-
highest activity for enzyme EII, EII' low activity
-
?
N-(8-aminooctanoyl)-6-aminohexanoic acid + H2O
8-aminooctanoic acid + 6-aminohexanoic acid
show the reaction diagram
-
low activity for enzyme EII, EII' no activity
-
?
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diisopropyl fluorophosphate
p-chloromercuribenzoate
-
inhibition at 0.013 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.9 - 220
N-(6-aminohexanoyl)-6-aminohexanoate
6.2
N-6-aminohexanoate-trimer
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
6-aminohexanoate trimer
-
-
2.4 - 19
N-(6-aminohexanoyl)-6-aminohexanoate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 9.5
-
same value for enzymes EII, EII'
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
-
2 * 42000, SDS-PAGE
84000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 42000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D181E
-
mutant with increased Km and decreased activity
D181N
-
mutant with increased Km and decreased activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
-
-
172042
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
stable for 1 h
50
-
EII most heat-stable
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogeneity, chromatography techniques, preparative gel electrophoresis
-
to homogeneity, chromatography techniques, recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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., Flavobacterium sp. KI72, Pseudomonas sp., Pseudomonas sp. NK87
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team