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Information on EC 3.5.1.117 - 6-aminohexanoate-oligomer endohydrolase 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 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).
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Flavobacterium sp.
UNIPROT: P07062
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Word Map
The taxonomic range for the selected organisms is: Flavobacterium sp.
The enzyme appears in selected viruses and cellular organisms
Synonyms
nylon hydrolase, 6-aminohexanoate-oligomer hydrolase, ald hydrolase, 6-aminohexanoic acid-oligomer hydrolase, nylon oligomer-hydrolyzing enzyme, 6-aminohexanoate-hydrolase, nylon-oligomer hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6-aminohexanoate-oligomer hydrolase
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-
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endo-type 6-aminohexanoate oligomer hydrolase
Q57326
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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).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
?
N-(6-aminohexanoyl)n-6-aminohexanoate + H2O
N-(6-aminohexanoyl)n-x + N-(6-aminohexanoyl)x-6-aminohexanoate
show the reaction diagram
-
-
-
?
nylon oligomer + H2O
?
show the reaction diagram
additional information
?
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negligible activity with N-(6-aminohexanoyl)-6-aminohexanoate and N-(6-aminohexanoyl)-N-(6-aminohexanoyl)-6-aminohexanoate and the cyclic dimer 1,8-diazacyclotetradecane-2,9-dione
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?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.3
pH 7.2, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27408
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
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
9000
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
9513
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kakudo, S.; Negoro, S.; Urabe, I.; Okada, H.
Nylon oligomer degradation gene, nylC, on plasmid pOAD2 from a Flavobacterium strain encodes endo-type 6-aminohexanoate oligomer hydrolase: purification and characterization of the nylC gene product
Appl. Environ. Microbiol.
59
3978-3980
1993
Flavobacterium sp. (Q79F77)
Manually annotated by BRENDA team
Negoro, S.; Kakudo, S.; Urabe, I.; Okada, H.
A new nylon oligomer degradation gene (nylC) on plasmid pOAD2 from a Flavobacterium sp.
J. Bacteriol.
174
7948-7953
1992
Flavobacterium sp. (Q79F77)
Manually annotated by BRENDA team
Kato, K.; Ohtsuki, K.; Koda, Y.; Maekawa, T.; Yomo, T.; Negoro, S.; Urabe, I.
A plasmid encoding enzymes for nylon oligomer degradation: nucleotide sequence and analysis of pOAD2
Microbiology
141
2585-2590
1995
Flavobacterium sp. (Q57326)
Manually annotated by BRENDA team