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Information on EC 3.5.2.12 - 6-aminohexanoate-cyclic-dimer hydrolase for references in articles please use BRENDA:EC3.5.2.12Word Map on EC 3.5.2.12
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The enzyme appears in viruses and cellular organisms
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6-aminohexanoate-cyclic-dimer hydrolase
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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
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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hydrolysis of cyclic amides
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hydrolysis
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nylon-6 oligomer degradation
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Caprolactam degradation
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Microbial metabolism in diverse environments
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1,8-diazacyclotetradecane-2,9-dione lactamhydrolase
The cyclic dimer of 6-aminohexanoate is converted to the linear dimer.
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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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6-aminohexanoate-cyclic-dimer hydrolase
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hydrolase, aminocaproate cyclic dimer
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Nylon oligomers degrading enzyme EI
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omega-laurolactam hydrolase
omega-laurolactam hydrolase
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omega-laurolactam hydrolase
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omega-laurolactam hydrolase
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omega-laurolactam hydrolase
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omega-laurolactam hydrolase
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omega-laurolactam hydrolase
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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)
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Achromobacter guttatus
KI72
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-
brenda
Achromobacter guttatus KI72
KI72
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brenda
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UniProt
brenda
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brenda
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UniProt
brenda
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UniProt
brenda
KI-72
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brenda
KI-72
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brenda
NK87
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brenda
NK87
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brenda
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UniProt
brenda
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brenda
formerly named Flavobacterium sp.
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brenda
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UniProt
brenda
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brenda
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1,8-diazacyclotetradecane-2,9-dione + H2O
N-(6-aminohexanoyl)-6-aminohexanoate
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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-
?
omega-laurolactam + H2O
12-aminolauric acid
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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-
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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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-
-
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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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-
?
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
assay at pH 7.0, 30°C, 48 h
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-
?
omega-laurolactam + H2O
12-aminolauric acid
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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
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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
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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
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?
omega-octalactam + H2O
?
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?
omega-octalactam + H2O
?
assay at pH 7.0, 30°C, 48 h
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?
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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
Achromobacter guttatus
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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
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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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-
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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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diisopropylphosphofluoridate
Hg2+
1 mM, complete enzyme inhibition
p-chloromercuribenzoate
Achromobacter guttatus
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10 mM
p-chloromercuribenzoic acid
1 mM, complete enzyme inhibition
diisopropylphosphofluoridate
Achromobacter guttatus
-
1 mM
diisopropylphosphofluoridate
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-
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0.6 - 6
1,8-Diazacyclotetradecane-2,9-dione
0.85 - 19
6-amino-hexanoate cyclic dimer
0.6
1,8-Diazacyclotetradecane-2,9-dione
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6
1,8-Diazacyclotetradecane-2,9-dione
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0.85
6-amino-hexanoate cyclic dimer
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mutant C316A, pH 7.0, 30°C
1.8
6-amino-hexanoate cyclic dimer
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mutant C316S, pH 7.0, 30°C
3.51
6-amino-hexanoate cyclic dimer
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wild-type, pH 7.0, 30°C
3.66
6-amino-hexanoate cyclic dimer
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mutant C316G, pH 7.0, 30°C
13.2
6-amino-hexanoate cyclic dimer
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mutant N125A, pH 7.0, 30°C
19
6-amino-hexanoate cyclic dimer
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mutant C316D, pH 7.0, 30°C
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8 - 10.7
1,8-Diazacyclotetradecane-2,9-dione
0.14 - 9.15
6-amino-hexanoate cyclic dimer
8
1,8-Diazacyclotetradecane-2,9-dione
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-
10.7
1,8-Diazacyclotetradecane-2,9-dione
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0.14
6-amino-hexanoate cyclic dimer
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mutant C316D, pH 7.0, 30°C
0.71
6-amino-hexanoate cyclic dimer
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mutant C316A, pH 7.0, 30°C
1.12
6-amino-hexanoate cyclic dimer
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mutant N125A, pH 7.0, 30°C
4.83
6-amino-hexanoate cyclic dimer
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mutant C316S, pH 7.0, 30°C
4.97
6-amino-hexanoate cyclic dimer
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wild-type, pH 7.0, 30°C
9.15
6-amino-hexanoate cyclic dimer
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mutant C316G, pH 7.0, 30°C
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0.007 - 2.68
6-amino-hexanoate cyclic dimer
0.007
6-amino-hexanoate cyclic dimer
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mutant C316D, pH 7.0, 30°C
0.085
6-amino-hexanoate cyclic dimer
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mutant N125A, pH 7.0, 30°C
0.83
6-amino-hexanoate cyclic dimer
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mutant C316A, pH 7.0, 30°C
1.42
6-amino-hexanoate cyclic dimer
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wild-type, pH 7.0, 30°C
2.5
6-amino-hexanoate cyclic dimer
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mutant C316G, pH 7.0, 30°C
2.68
6-amino-hexanoate cyclic dimer
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mutant C316S, pH 7.0, 30°C
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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
-
mutant C316A, pH 7.0, 30°C
1.29
-
assay at 30°C, total incubation time 20 h
2.77
-
assay at 30°C, total incubation time 20 h
4.1
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wild-type, pH 7.0, 30°C
4.46
-
mutant C316S, pH 7.0, 30°C
7.7
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mutant C316G, pH 7.0, 30°C
8.26
-
assay at 37°C, incubation for 12 h
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7.2
potassium phosphate buffer, 45°C
7
-
assay at
7.3
Achromobacter guttatus
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-
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5.5 - 8.5
Achromobacter guttatus
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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
30
-
assay at
33
Achromobacter guttatus
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-
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brenda
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brenda
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brenda
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brenda
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brenda
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Flavobacterium sp. (strain K172);
P13398
Flavobacterium sp. (strain K172);
P13398
Flavobacterium sp. (strain K172);
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55000
Achromobacter guttatus
-
2 * 55000, SDS-PAGE
110000
-
gel filtration
110000
Achromobacter guttatus
-
gel filtration
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dimer
Achromobacter guttatus
-
2 * 55000, SDS-PAGE
dimer
Achromobacter guttatus KI72
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2 * 55000, SDS-PAGE
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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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-
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35
30 min, stable up to 35°C
40
30 min, 20% loss of activity
45
30 min, 80% loss of activity
48
-
half life of 1.6 min
50
30 min, completely inactivated
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Hi-Trap Q-Sepharose column chromatography
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-
-
-
Achromobacter guttatus
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expressed in Escherichia coli
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expression in Escherichia coli
overexpression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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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
-
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
-
3.6% of wild-type activity
C316N
-
4.3% of wild-type activity
C316S
-
107% of wild-type activity
K72A
-
decreases the hydrolytic and esterolytic activities to undetectable levels
N125A
-
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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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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