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Literature summary extracted from

  • Kamiya, K.; Baba, T.; Boero, M.; Matsui, T.; Negoro, S.; Shigeta, Y.
    Nylon-oligomer hydrolase promoting cleavage reactions in unnatural amide compounds (2014), J. Phys. Chem. Lett., 5, 1210-1216.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.117 [N-(6-aminohexanoyl)]n + H2O Arthrobacter sp.
-
 [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
-
 ?
3.5.1.117 [N-(6-aminohexanoyl)]n + H2O Arthrobacter sp. KI72
-
 [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.117 Arthrobacter sp.
-
-
-
3.5.1.117 Arthrobacter sp. KI72
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.1.117 [N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x NylB active site with a tyrosine residue Tyr170, cleavage mechanism of the Ald amide bond in acylation of NylB is as a two-step reaction, various intermediate states, catalytic mechanism, hybrid QM/MM dynamics in combination with free-energy sampling simulations, detailed overview Arthrobacter sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.117 [N-(6-aminohexanoyl)]n + H2O
-
 Arthrobacter sp. [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
-
 ?
3.5.1.117 [N-(6-aminohexanoyl)]n + H2O
-
 Arthrobacter sp. KI72 [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.117 6-aminohexanoate-dimer hydrolase
-
 Arthrobacter sp.
3.5.1.117 Ahx-linear-dimer hydrolase
-
 Arthrobacter sp.
3.5.1.117 Ald hydrolase
-
 Arthrobacter sp.
3.5.1.117 endotype Ahx-oligomer hydrolase
-
 Arthrobacter sp.
3.5.1.117 NylB
-
 Arthrobacter sp.
3.5.1.117 NylB-type nylon-oligomer hydrolase
-
 Arthrobacter sp.
3.5.1.117 NylC
-
 Arthrobacter sp.
3.5.1.117 nylon-oligomer hydrolase
-
 Arthrobacter sp.

General Information

EC Number General Information Comment Organism
3.5.1.117 evolution the active site of 6-aminohexanoate-dimer hydrolase, a nylon-6 byproduct-degrading enzyme with a beta-lactamase fold, possesses a Ser112/Lys115/Tyr215 catalytic triad similar to the one of penicillin-recognizing family of serine-reactive hydrolases but includes a unique Tyr170 residue. Three types of nylon-oligomer hydrolases: Ahx-cyclic-dimer hydrolase exist: (NylA), Ahx-linear-dimer (Ald) hydrolase (NylB), and endotype Ahx-oligomer hydrolase (NylC) Arthrobacter sp.
3.5.1.117 additional information the active site of 6-aminohexanoate-dimer hydrolase, a nylon-6 byproduct-degrading enzyme with a beta-lactamase fold, possesses a Ser112/Lys115/Tyr215 catalytic triad similar to the one of penicillin-recognizing family of serinereactive hydrolases but includes a unique Tyr170 residue Arthrobacter sp.
3.5.1.117 additional information the enzyme can adopt two different conformations: a substrate-free form (open form) and a substrate-bound form (closed from), hybrid quantum mechanics/molecular mechanics (QM/MM) dynamical simulations complemented with free energy sampling methods, allow to determine the reaction mechanismin NylB and address one of the possible roles of Tyr170 during the acylation process, enzyme structure and induced-fit process, detailed overview Arthrobacter sp.