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Literature summary for 3.5.1.117 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
Search for more literature for 3.5.1.117

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Arthrobacter sp.
-
-
-
Arthrobacter sp. KI72
-
-
-

Reaction

Reaction Comment Organism Reaction ID
[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)

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

Synonyms

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

General Information

General Information Comment Organism
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.
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.
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.