Information on EC 3.5.2.12 - 6-aminohexanoate-cyclic-dimer hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.2.12
-
RECOMMENDED NAME
GeneOntology No.
6-aminohexanoate-cyclic-dimer hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1,8-diazacyclotetradecane-2,9-dione + H2O = N-(6-aminohexanoyl)-6-aminohexanoate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
hydrolysis of cyclic amides
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Caprolactam degradation
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Microbial metabolism in diverse environments
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nylon-6 oligomer degradation
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Achromobacter guttatus
KI72
-
-
Manually annotated by BRENDA team
Achromobacter guttatus KI72
KI72
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
show the reaction diagram
6-amino-hexanoate cyclic dimer + H2O
6-aminohexanoate linear dimer
show the reaction diagram
-
-
-
-
?
6-amino-hexanoate-cyclic-dimer + H2O
?
show the reaction diagram
assay at pH 7.0, 30°C, 48 h
-
-
?
omega-laurolactam + H2O
12-aminolauric acid
show the reaction diagram
omega-octalactam + H2O
?
show the reaction diagram
additional information
?
-
-
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diisopropylphosphofluoridate
Hg2+
1 mM, complete enzyme inhibition
p-chloromercuribenzoate
Achromobacter guttatus
-
10 mM
p-chloromercuribenzoic acid
1 mM, complete enzyme inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6 - 6
1,8-Diazacyclotetradecane-2,9-dione
0.85 - 19
6-amino-hexanoate cyclic dimer
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8 - 10.7
1,8-Diazacyclotetradecane-2,9-dione
0.14 - 9.15
6-amino-hexanoate cyclic dimer
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007 - 2.68
6-amino-hexanoate cyclic dimer
5867
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.04
-
mutant C316E, pH 7.0, 30°C
0.063
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mutant C316D, pH 7.0, 30°C
0.15
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mutant C316K, pH 7.0, 30°C
0.18
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mutant C316N, pH 7.0, 30°C
0.29
-
assay at 30°C, total incubation time 20 h
0.36
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assay at 30°C, total incubation time 20 h
0.57
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mutant N125A, pH 7.0, 30°C
0.73
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mutant C316A, pH 7.0, 30°C
1.29
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assay at 30°C, total incubation time 20 h
2.77
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assay at 30°C, total incubation time 20 h
4.1
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wild-type, pH 7.0, 30°C
4.46
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mutant C316S, pH 7.0, 30°C
7.7
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mutant C316G, pH 7.0, 30°C
8.26
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assay at 37°C, incubation for 12 h
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
potassium phosphate buffer, 45°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at 30°C and incubation time of 20 h, assay at 37°C and incubation time of 12 h
45
pH around 7.2 in potassium phosphate buffer
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
Achromobacter guttatus
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2 * 55000, SDS-PAGE
79500
gel chromatography
110000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1 - 8.2
30°C
696817
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
30 min, stable up to 35°C
40
30 min, 20% loss of activity
45
30 min, 80% loss of activity
48
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half life of 1.6 min
50
30 min, completely inactivated
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hi-Trap Q-Sepharose column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expression in Escherichia coli
overexpression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
C316D
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1.5% of wild-type activity
C316E
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1%% of wild-type activity
C316G
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185% of wild-type activity
C316K
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3.6% of wild-type activity
C316N
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4.3% of wild-type activity
C316S
-
107% of wild-type activity
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
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decreases the hydrolytic and esterolytic activities to undetectable levels
S174A
-
decreases the hydrolytic and esterolytic activities to undetectable levels
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