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Literature summary for 3.5.1.117 extracted from

  • Yasuhira, K.; Tanaka, Y.; Shibata, H.; Kawashima, Y.; Ohara, A.; Kato, D.; Takeo, M.; Negoro, S.
    6-Aminohexanoate oligomer hydrolases from the alkalophilic bacteria Agromyces sp. strain KY5R and Kocuria sp. strain KY2 (2007), Appl. Environ. Microbiol., 73, 7099-7102.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.117

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Agromyces sp.
expression in Escherichia coli Kocuria sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 6-aminohexanoate cyclic oligomer Km-value for 6-aminohexanoate cyclic oligomer: 0.44 mg/ml, pH 7.0, 30°C Kocuria sp.
additional information
-
 6-aminohexanoate cyclic oligomer Km-value for 6-aminohexanoate cyclic oligomer: 0.49 mg/ml, pH 7.0, 30°C Agromyces sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
9000
-
 x * 27000 + x * 9000, SDS-PAGE Agromyces sp.
9000
-
 x * 27000 + x * 9000, SDS-PAGE Kocuria sp.
27000
-
 x * 27000 + x * 9000, SDS-PAGE Agromyces sp.
27000
-
 x * 27000 + x * 9000, SDS-PAGE Kocuria sp.

Organism

Organism UniProt Comment Textmining
Agromyces sp. Q1EPR5
-
-
Agromyces sp. KY5R Q1EPR5
-
-
Kocuria sp. Q1EPR4
-
-
Kocuria sp. KY2 Q1EPR4
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Agromyces sp.
-
 Kocuria sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6-aminohexanoate cyclic oligomer + H2O degree of polymerization > 3. The enzyme produces 6-aminohexanoate from Ahx cyclic oligomers (the NylC-specific substrate) but give no detectable amounts of reaction products from either the 6-aminohexanoate cyclic dimer or the 6-aminohexanoate linear dimer Kocuria sp. 6-aminohexanoate
-
 ?
6-aminohexanoate cyclic oligomer + H2O degree of polymerization > 3. The enzyme produces 6-aminohexanoate from Ahx cyclic oligomers (the NylC-specific substrate) but give no detectable amounts of reaction products from either the 6-aminohexanoate cyclic dimer or the 6-aminohexanoate linear dimer Kocuria sp. KY2 6-aminohexanoate
-
 ?
6-aminohexanoate cyclic oligomer + H2O degree of polymerization > 3. The enzyme produces 6-aminohexanoate from Ahx cyclic oligomers (the NylC-specific substrate) but give no detectable amounts of reaction products from either the 6-aminohexanoate cyclic dimer or the 6-aminohexanoate linear dimer Agromyces sp. ?
-
 ?
6-aminohexanoate cyclic oligomer + H2O degree of polymerization > 3. The enzyme produces 6-aminohexanoate from Ahx cyclic oligomers (the NylC-specific substrate) but give no detectable amounts of reaction products from either the 6-aminohexanoate cyclic dimer or the 6-aminohexanoate linear dimer Agromyces sp. KY5R ?
-
 ?
nylon oligomer + H2O
-
 Agromyces sp. ?
-
 ?
nylon oligomer + H2O
-
 Kocuria sp. ?
-
 ?
nylon oligomer + H2O
-
 Kocuria sp. KY2 ?
-
 ?
nylon oligomer + H2O
-
 Agromyces sp. KY5R ?
-
 ?

Subunits

Subunits Comment Organism
? x * 27000 + x * 9000, SDS-PAGE Agromyces sp.
? x * 27000 + x * 9000, SDS-PAGE Kocuria sp.

Synonyms

Synonyms Comment Organism
Ahx endo-type-oligomer hydrolase
-
 Agromyces sp.
Ahx endo-type-oligomer hydrolase
-
 Kocuria sp.
NylC
-
 Agromyces sp.
NylC
-
 Kocuria sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 assay at Agromyces sp.
60
-
 assay at Kocuria sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
 30 min, enzyme retains 90% of its activity Agromyces sp.
60
-
 30 min, enzyme retains 90% of its activity Kocuria sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
 assay at Agromyces sp.
7.3
-
 assay at Kocuria sp.
7.5
-
-
 Agromyces sp.
8
-
-
 Kocuria sp.