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Literature summary for 3.5.1.46 extracted from

  • Ohki, T.; Wakitani, Y.; Takeo, M.; Yasuhira, K.; Shibata, N.; Higuchi, Y.; Negoro, S.
    Mutational analysis of 6-aminohexanoate-dimer hydrolase: relationship between nylon oligomer hydrolytic and esterolytic activities (2006), FEBS Lett., 580, 5054-5058.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
nylB24 gene, expression of the His-tagged EII-EII'-hybrid Hyb24 in Escherichia coli strain KP3998 Arthrobacter sp.

Protein Variants

Protein Variants Comment Organism
A61V/A253T/F264C/D370Y site-directed mutagenesis, 10fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate Arthrobacter sp.
T3A/P4R/T5S/S8Q/D15G site-directed mutagenesis, 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.
T3A/P4R/T5S/S8Q/D15G/D370Y site-directed mutagenesis, mutant Hyb24, by five amino acid replacement in EII' for residues of EII, plus 2 additional exchanges for EII residues leading to a 10fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate Arthrobacter sp.
T3A/P4R/T5S/S8Q/D15G/G181D site-directed mutagenesis, mutant Hyb24, by five amino acid replacement in EII' for residues of EII, plus 2 additional exchanges for EII residues leading to a 10fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate Arthrobacter sp.
T3A/P4R/T5S/S8Q/D15G/G181D/D370Y site-directed mutagenesis, mutant Hyb24, by five amino acid replacement in EII' for residues of EII, plus 2 additional exchanges for EII residues leading to a 100fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate Arthrobacter sp.

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Arthrobacter sp.
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formerly Flavobacterium sp., strain K172, enzyme form EII and cryptic enzyme form EII'
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Reaction

Reaction Comment Organism Reaction ID
N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate structure-function relationship, residues 370 and 181 are imporatant for enzyme activity Arthrobacter sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-(6-aminohexanoyl)-6-aminohexanoate + H2O the enzyme is responsible for the degradation of nylon-6 industrial production by-products Arthrobacter sp. 6-aminohexanoate
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N-(6-aminohexanoyl)-6-aminohexanoate + H2O the enzyme hydrolyzes the linear dimer substrate Arthrobacter sp. 6-aminohexanoate
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