KEGG   ORTHOLOGY: K01453
Entry
K01453                      KO                                     
Symbol
nylB
Name
6-aminohexanoate-oligomer exohydrolase [EC:3.5.1.46]
Pathway
map00930  Caprolactam degradation
map01120  Microbial metabolism in diverse environments
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09111 Xenobiotics biodegradation and metabolism
   00930 Caprolactam degradation
    K01453  nylB; 6-aminohexanoate-oligomer exohydrolase
Enzymes [BR:ko01000]
 3. Hydrolases
  3.5  Acting on carbon-nitrogen bonds, other than peptide bonds
   3.5.1  In linear amides
    3.5.1.46  6-aminohexanoate-oligomer exohydrolase
     K01453  nylB; 6-aminohexanoate-oligomer exohydrolase
Other DBs
RN: R00059 R10975 R10979
GO: 0019875
Genes
NSM: JO391_02540
AMAU: DSM26151_03960(nylB')
LEU: Leucomu_04960
LTR: EVS81_02965
LLUT: K1X41_10430
ARR: ARUE_c40930(nylB)
AAU: AAur_3953(nylB)
NDK: I601_2859(nylB')
AG: BAA05087(nylB) BAA05089(nylB')
Reference
  Authors
Negoro S
  Title
Biodegradation of nylon oligomers.
  Journal
Appl Microbiol Biotechnol 54:461-6 (2000)
DOI:10.1007/s002530000434
  Sequence
Reference
PMID:6646204
  Authors
Okada H, Negoro S, Kimura H, Nakamura S
  Title
Evolutionary adaptation of plasmid-encoded enzymes for degrading nylon oligomers.
  Journal
Nature 306:203-6 (1983)
DOI:10.1038/306203a0
  Sequence

KEGG   ENZYME: 3.5.1.46
Entry
EC 3.5.1.46                 Enzyme                                 
Name
6-aminohexanoate-oligomer exohydrolase;
6-aminohexanoate-dimer hydrolase;
nylB (gene name);
6-aminohexanoic acid oligomer hydrolase (ambiguous);
N-(6-aminohexanoyl)-6-aminohexanoate amidohydrolase;
nylon-6 hydrolase (ambiguous)
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
Sysname
N-(6-aminohexanoyl)-6-aminohexanoate exoamidohydrolase
Reaction(IUBMB)
(1) [N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-1 + 6-aminohexanoate [RN:R10975];
(2) N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate [RN:R00059]
Reaction(KEGG)
R00059 R10975;
(other) R10979
Substrate
[N-(6-aminohexanoyl)]n [CPD:C20988];
H2O [CPD:C00001];
N-(6-aminohexanoyl)-6-aminohexanoate [CPD:C01255]
Product
[N-(6-aminohexanoyl)]n-1;
6-aminohexanoate [CPD:C02378]
Comment
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.
History
EC 3.5.1.46 created 1983, modified 2014
Pathway
ec00930  Caprolactam degradation
ec01120  Microbial metabolism in diverse environments
Orthology
K01453  6-aminohexanoate-oligomer exohydrolase
Genes
NSMJO391_02540
AMAUDSM26151_03960(nylB')
LEULeucomu_04960
LTREVS81_02965
LLUTK1X41_10430
ARRARUE_c40930(nylB)
AAUAAur_3953(nylB)
NDKI601_2859(nylB')
Reference
1  [PMID:7262074]
  Authors
Kinoshita S, Terada T, Taniguchi T, Takene Y, Masuda S, Matsunaga N, Okada H.
  Title
Purification and characterization of 6-aminohexanoic-acid-oligomer hydrolase of Flavobacterium sp. Ki72.
  Journal
Eur J Biochem 116:547-51 (1981)
DOI:10.1111/j.1432-1033.1981.tb05371.x
Other DBs
ExplorEnz - The Enzyme Database: 3.5.1.46
IUBMB Enzyme Nomenclature: 3.5.1.46
ExPASy - ENZYME nomenclature database: 3.5.1.46
UM-BBD (Biocatalysis/Biodegradation Database): 3.5.1.46
BRENDA, the Enzyme Database: 3.5.1.46
CAS: 75216-15-8

KEGG   REACTION: R00059
Entry
R00059                      Reaction                               
Name
N-(6-aminohexanoyl)-6-aminohexanoate amidohydrolase
Definition
N-(6-Aminohexanoyl)-6-aminohexanoate + H2O <=> 2 6-Aminohexanoate
Equation
Reaction class
RC00090  C01255_C02378
RC00096  C01255_C02378
Enzyme
Pathway
rn00930  Caprolactam degradation
rn01120  Microbial metabolism in diverse environments
Orthology
K01453  6-aminohexanoate-oligomer exohydrolase [EC:3.5.1.46]
Other DBs
RHEA: 21367

DBGET integrated database retrieval system