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Information on EC 3.5.2.12 - 6-aminohexanoate-cyclic-dimer hydrolase
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3.5.2.12 6-aminohexanoate-cyclic-dimer hydrolaseIUBMB Comments
The cyclic dimer of 6-aminohexanoate is converted to the linear dimer.
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Word Map
- 3.5.2.12
- pyrimidine
- dhoase
-
3.5.2.3
-
carbamyl
- l-dihydroorotate
-
transcarbamoylase
-
amidohydrolase
-
n-carbamyl-l-aspartate
- atcase
-
trifunctional
-
aeolicus
-
aquifex
-
oroticum
-
glutamine-dependent
- carbamoyl-phosphate
- dihydropyrimidinase
-
christopherson
-
2.1.3.2
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
omega-laurolactam hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-aminohexanoate-cyclic- dimer hydrolase (Caulobacter crescentus gene CC1323)
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6-aminohexanoate-cyclic- dimer hydrolase (Deinococcus radiodurans strain R1 gene DR0235)
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hydrolase, aminocaproate cyclic dimer
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Nylon oligomers degrading enzyme EI
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omega-laurolactam hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1,8-diazacyclotetradecane-2,9-dione + H2O = N-(6-aminohexanoyl)-6-aminohexanoate
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1,8-diazacyclotetradecane-2,9-dione + H2O = N-(6-aminohexanoyl)-6-aminohexanoate
a Ser174-cis-Ser150-Lys72 triad constitutes the catalytic center, the backbone N in Ala171 and Ala172 are involved in oxyanion stabilization, Cys316-S forms a hydrogen bond with nitrogen N7 of 6-amino-hexanoate cyclic dimer at the uncleaved amide bond in two equivalent amide bonds of 6-amino-hexanoate cyclic dimer
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of cyclic amides
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-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
1,8-diazacyclotetradecane-2,9-dione lactamhydrolase
The cyclic dimer of 6-aminohexanoate is converted to the linear dimer.
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CAS REGISTRY NUMBER
COMMENTARY
250298-92-1
6-aminohexanoate-cyclic- dimer hydrolase (Deinococcus radiodurans strain R1 gene DR0235)
332972-89-1
6-aminohexanoate-cyclic- dimer hydrolase (Caulobacter crescentus gene CC1323)
60976-29-6
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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
6-amino-hexanoate cyclic dimer + H2O
6-aminohexanoate linear dimer
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?
6-amino-hexanoate-cyclic-dimer + H2O
?
assay at pH 7.0, 30°C, 48 h
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?
additional information
?
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enzyme additionally catalyzes the hydrolysis of amide compounds and esters such as glutamine, malonamide, indoleacetamide, 4-nitrophenylacetate, with a specific activity beolw 0.5% of the activity with 6-amino-hexanoate cyclic dimer
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1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
Achromobacter guttatus
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-
-
-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
Achromobacter guttatus
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i.e. 6-aminohexanoic acid cyclic dimer
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-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
Achromobacter guttatus KI72
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-
-
-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
Achromobacter guttatus KI72
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i.e. 6-aminohexanoic acid cyclic dimer
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-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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-
-
-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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-
-
-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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i.e. 6-aminohexanoic acid cyclic dimer
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-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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-
-
-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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i.e. 6-aminohexanoic acid cyclic dimer
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-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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-
-
-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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i.e. 6-aminohexanoic acid cyclic dimer
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-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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-
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-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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i.e. 6-aminohexanoic acid cyclic dimer
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-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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-
-
-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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i.e. 6-aminohexanoic acid cyclic dimer
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-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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-
-
-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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i.e. 6-aminohexanoic acid cyclic dimer
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-
?
omega-laurolactam + H2O
12-aminolauric acid
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assay at 30°C, total incubation time 20 h
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?
omega-laurolactam + H2O
12-aminolauric acid
B7XBZ8
assay at pH 7.0, 30°C, 48 h
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-
?
omega-laurolactam + H2O
12-aminolauric acid
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assay at 30°C, total incubation time 20 h
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-
?
omega-laurolactam + H2O
12-aminolauric acid
assay at pH 7.0, 30°C, 48 h
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-
?
omega-laurolactam + H2O
12-aminolauric acid
-
assay at 30°C, total incubation time 20 h
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-
?
omega-laurolactam + H2O
12-aminolauric acid
assay at pH 7.0, 30°C, 48 h
-
-
?
omega-laurolactam + H2O
12-aminolauric acid
-
assay at 30°C, total incubation time 20 h
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-
?
omega-laurolactam + H2O
12-aminolauric acid
assay at pH 7.0, 30°C, 48 h
-
-
?
omega-laurolactam + H2O
12-aminolauric acid
-
assay at 30°C, total incubation time 20 h
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-
?
omega-laurolactam + H2O
12-aminolauric acid
assay at pH 7.0, 30°C, 48 h
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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
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
Achromobacter guttatus
-
-
-
-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
Achromobacter guttatus KI72
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-
-
-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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-
-
-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
-
-
-
-
?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
-
-
-
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?
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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-
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?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
33
37
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assay at 30°C and incubation time of 20 h, assay at 37°C and incubation time of 12 h
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (498 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
Achromobacter guttatus KI72
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2 * 55000, SDS-PAGE
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method with sodium citrate as precipitant in imidazole buffer pH 8.0
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single anonymous dispersion phasing of mercury derivative to 2.2 A, and construction of models of the native enzyme and mutant S174A to 1.9 A resolution. The overall structure of the molecule is a compact mixed alpha/beta fold containing a central irregular-sheet composed of 11 beta-strands surrounded by 20 alpha-helices
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C316A
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18% of wild-type hydrolytic activity, decrease in the Km to approximately one-quarter the level of wild-type NylA, CD spectra similar to wild-type
K72A
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decreases the hydrolytic and esterolytic activities to undetectable levels
N125A
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14% of wild-type hydrolytic activity, CD spectra similar to wild-type
S150A
-
decreases the hydrolytic and esterolytic activities to undetectable levels
S174A
-
decreases the hydrolytic and esterolytic activities to undetectable levels
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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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
Pseudomonas sp., Pseudomonas sp. NK87
brenda
Kinoshita, S.
Microbial degradation of 6-aminohexanoic acid cyclic dimer and its enzymes
Hakko Kogaku Kaishi
60
363-375
1982
Flavobacterium sp., Flavobacterium sp. KI-72
-
brenda
Negoro, S.; Shinagawa, H.; Nakata, A.; Kinoshita, S.; Hatozaki, T.; Okada, H.
Plasmid control of 6-aminohexanoic acid cyclic dimer degradation enzymes of Flavobacterium sp. KI72
J. Bacteriol.
143
238-245
1980
Flavobacterium sp., Flavobacterium sp. KI-72
brenda
Kinoshita, S.; Negoro, S.; Muramatso, M.; Bisaria, V.S.; Sawada, S.; Okada, H.
6-Aminohexanoic acid cyclic dimer hydrolase. A new cyclic amide hydrolase produced by Achromobacter guttatus KI72
Eur. J. Biochem.
80
489-495
1977
Achromobacter guttatus, Achromobacter guttatus KI72
brenda
Tsuchiya, K.; Fukuyama, S.; Kanzaki, N.; Kanagawa, K.; Negoro, S.; Okada, H.
High homology between 6-aminohexnoate-cyclic-dimer hydrolases of Flavobacterium and Pseudomonas strains
J. Bacteriol.
171
3187-3191
1989
Flavobacterium sp., Flavobacterium sp. KI-72, Pseudomonas sp., Pseudomonas sp. NK87
brenda
Kanagawa, K.; Negoro, S.; Takada, N.; Okada, H.
Plasmid dependence of Pseudomonas sp. NK87 enzymes that degrade 6-aminohexanoate-cyclic dimer
J. Bacteriol.
171
3181-3186
1989
Pseudomonas sp., Pseudomonas sp. NK87
brenda
Yasuhira, K.; Uedo, Y.; Shibata, N.; Negoro, S.; Takeo, M.; Higuchi, Y.
Crystallization and X-ray diffraction analysis of 6-aminohexanoate-cyclic-dimer hydrolase from Arthrobacter sp. KI72
Acta Crystallogr. Sect. F
62
1209-1211
2006
Arthrobacter sp.
brenda
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
Arthrobacter sp.
brenda
Asano, Y.; Fukuta, Y.; Yoshida, Y.; Komeda, H.
The screening, characterization, and use of omega-laurolactam hydrolase: a new enzymatic synthesis of 12-aminolauric acid
Biosci. Biotechnol. Biochem.
72
2141-2150
2008
Acidovorax sp. T31 (B7XBZ8), Cupriavidus sp. T7 (B7XBZ7), Cupriavidus sp. U124 (B7XBZ9), Rhodococcus sp. U-224 (B5MF68), Sphingomonas sp. U238 (B7XC00)
brenda
Fukuta, Y.; Komeda, H.; Yoshida, Y.; Asano, Y.
High yield synthesis of 12-aminolauric acid by 'enzymatic transcrystallization' of omega-laurolactam using omega-laurolactam hydrolase from acidovorax sp. T31
Biosci. Biotechnol. Biochem.
73
80551-1 - 7
2009
Acidovorax sp. T31 (B7XBZ8), Arthrobacter sp. KI72, Cupriavidus sp. T7 (B7XBZ7), Cupriavidus sp. U124 (B7XBZ9), Rhodococcus sp. U-224, Sphingomonas sp. U238 (B7XC00)
brenda
Yasuhira, K.; Shibata, N.; Mongami, G.; Uedo, Y.; Atsumi, Y.; Kawashima, Y.; Hibino, A.; Tanaka, Y.; Lee, Y.H.; Kato, D.; Takeo, M.; Higuchi, Y.; Negoro, S.
X-ray crystallographic analysis of the 6-aminohexanoate cyclic dimer hydrolase: catalytic mechanism and evolution of an enzyme responsible for nylon-6 byproduct degradation
J. Biol. Chem.
285
1239-1248
2010
Arthrobacter sp. KI72
brenda
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