KEGG   ENZYME: 3.5.1.117
Entry
EC 3.5.1.117                Enzyme                                 
Name
6-aminohexanoate-oligomer endohydrolase;
endo-type 6-aminohexanoate oligomer hydrolase;
Ahx endo-type-oligomer hydrolase;
6-aminohexanoate oligomer hydrolase;
Ahx-oligomer hydrolase;
nylon hydrolase;
nylon-oligomer hydrolase;
NylC;
nylon-6 hydrolase (ambiguous)
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
Sysname
6-aminohexanoate oligomer endoamidohydrolase
Reaction(IUBMB)
[N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x [RN:R10976]
Reaction(KEGG)
R10976;
(other) R10978 R10979
Substrate
[N-(6-aminohexanoyl)]n [CPD:C20988];
H2O [CPD:C00001]
Product
[N-(6-aminohexanoyl)]n-x;
[N-(6-aminohexanoyl)]x
Comment
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).
History
EC 3.5.1.117 created 2014
Pathway
ec00930  Caprolactam degradation
ec01120  Microbial metabolism in diverse environments
Orthology
K19963  6-aminohexanoate-oligomer endohydrolase
Genes
GSOPH603_12665
MICRBMW26_04430
MRNK8F61_06370
MICSC1N74_01735
ASOIMTP13_02070 MTP13_02075 MTP13_02450
LTREVS81_05135
LRPMUN76_07125
AGGC1N71_00300
GSDM3M28_12475
SGRGL0C25_05825
ACTWF7P10_35555
NOABKM31_31370
NGNLCN96_13830
NFSOIE67_33265
AMYYYIM_16760
PMADBAY61_11955
MICHFJK98_13105
MCABHXZ27_01495
MENOJiend_13290
CALNNIES2098_53370
 » show all
Reference
1  [PMID:8285701]
  Authors
Kakudo S, Negoro S, Urabe I, Okada H
  Title
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.
  Journal
Appl Environ Microbiol 59:3978-80 (1993)
DOI:10.1128/AEM.59.11.3978-3980.1993
Reference
2  [PMID:17827307]
  Authors
Yasuhira K, Tanaka Y, Shibata H, Kawashima Y, Ohara A, Kato D, Takeo M, Negoro S
  Title
6-Aminohexanoate oligomer hydrolases from the alkalophilic bacteria Agromyces sp. strain KY5R and Kocuria sp. strain KY2.
  Journal
Appl Environ Microbiol 73:7099-102 (2007)
DOI:10.1128/AEM.00777-07
Reference
3  [PMID:22187439]
  Authors
Negoro S, Shibata N, Tanaka Y, Yasuhira K, Shibata H, Hashimoto H, Lee YH, Oshima S, Santa R, Oshima S, Mochiji K, Goto Y, Ikegami T, Nagai K, Kato D, Takeo M, Higuchi Y
  Title
Three-dimensional structure of nylon hydrolase and mechanism of nylon-6 hydrolysis.
  Journal
J Biol Chem 287:5079-90 (2012)
DOI:10.1074/jbc.M111.321992
Other DBs
ExplorEnz - The Enzyme Database: 3.5.1.117
IUBMB Enzyme Nomenclature: 3.5.1.117
ExPASy - ENZYME nomenclature database: 3.5.1.117
BRENDA, the Enzyme Database: 3.5.1.117

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