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Literature summary extracted from

  • Negoro, S.; Ohki, T.; Shibata, N.; Mizuno, N.; Wakitani, Y.; Tsurukame, J.; Matsumoto, K.; Kawamoto, I.; Takeo, M.; Higuchi, Y.
    X-ray crystallographic analysis of 6-aminohexanoate-dimer hydrolase: molecular basis for the birth of a nylon oligomer-degrading enzyme (2005), J. Biol. Chem., 280, 39644-39652.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.46 expression of the His-tagged EII and the EII-EII'-hybrid Hyb24 in Escherichia coli strains JM109 and KP3998, respectively Arthrobacter sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.46 purified recombinant Hyb24 by sitting drop vapor diffusion from 0.1 M MES, pH 6.5, 2.0–2.2 M ammonium sulfate, 0.1–0.2 M lithium sulfate, at 10°C, 2 ml of sample mixed with 2 ml of reservoir solution, preparation of HgCl2 heavy atom derivatives, X-ray diffraction structure determination and analysis at 1.8 A resolution Arthrobacter sp.

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.46 D181E site-directed mutagenesis of EII, the mutant shows reduced activity compared to the wild-type enzyme Arthrobacter sp.
3.5.1.46 D181H site-directed mutagenesis of EII, the mutant shows highly reduced activity compared to the wild-type enzyme Arthrobacter sp.
3.5.1.46 D181K site-directed mutagenesis of EII, nearly inactive mutant Arthrobacter sp.
3.5.1.46 D181N site-directed mutagenesis of EII, the mutant shows reduced activity compared to the wild-type enzyme Arthrobacter sp.
3.5.1.46 T3A/P4R/T5S/S8Q/D15G construction of a hybrid of isozymes EII and EII', termed Hyb24, by five amino acid replacement in EII', the mutant shows the same activity as EII' Arthrobacter sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.46 N-(6-aminohexanoyl)-6-aminohexanoate + H2O Arthrobacter sp. the enzyme is responsible for the degradation of nylon-6 industrial production by-products 6-aminohexanoate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.46 Arthrobacter sp.
-
 formerly Flavobacterium sp., strain K172, enzyme form EII and cryptic enzyme form EII'
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.46 recombinant His-tagged EII from Escherichia coli strain by nickel affinity chromatography, recombinant EII-EII'-hybrid Hyb24 from Escherichia coli strain KP3998 by anion exchange chromatography, gel filtration, and again anion exchange chromatography, both enzymes to homogeneity Arthrobacter sp.

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.1.46 N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate Ser112 is a nucleophilic catalytic residue, Asp181 and Asn226 are also required Arthrobacter sp.
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.1.46 4.16
-
 purified recombinant wild-type EII Arthrobacter sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.46 4-nitrophenyl acetate + H2O
-
 Arthrobacter sp. 4-nitrophenol + acetate
-
 ?
3.5.1.46 4-nitrophenylbutyrate + H2O
-
 Arthrobacter sp. 4-nitrophenol + butyrate
-
 ?
3.5.1.46 additional information substrate specificity of EII and mutant Hyb24, no activity with D-Ala-D-Ala Arthrobacter sp. ?
-
 ?
3.5.1.46 N-(6-aminohexanoyl)-6-aminohexanoate + H2O the enzyme is responsible for the degradation of nylon-6 industrial production by-products Arthrobacter sp. 6-aminohexanoate
-
 ?
3.5.1.46 N-(6-aminohexanoyl)-6-aminohexanoate + H2O isozyme EII' shows only about 0.5% of the activity of EII Arthrobacter sp. 6-aminohexanoate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.46 More analysis of domain structures of EII, cryptic enzyme form EII', and EII-EII'-hybrid Hyb24 Arthrobacter sp.

Synonyms

EC Number Synonyms Comment Organism
3.5.1.46 nylon oligomer hydrolase
-
 Arthrobacter sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.46 30
-
 assay at Arthrobacter sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.46 7
-
 assay at Arthrobacter sp.