EC Number   |
General Information |
Reference |
|---|
   3.5.1.117 | evolution |
enzyme NylC is a member of the N-terminal nucleophile hydrolase superfamily |
733191 |
| 3.5.1.117 | evolution |
NylB belongs to the class C of the beta-lactamase family, which is characterized by the presence of a catalytic triad, namely, Ser, Tyr, and Lys, having the ability to promote the hydrolysis of amide and/or ester bonds. Natural selection is responsible for the development of the peculiar hydrolytic activity of Arthrobacter sp. KI72 |
-, 734851 |
| 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) |
-, 730264 |
| 3.5.1.117 | metabolism |
enzymatic degradation of 6-aminohexanoate and its oligomers in Arthrobacter sp. KI7 by the Nyl enzymes. A 6-aminohexanoate oligomer is converted to adipate, pathway overview. 6-Aminohexanoate oligomers are almost completely converted to the monomers (Ahx) by the three nylon oligomer-degrading enzymes, NylA, NylB, and NylC. 6-Aminohexanoate aminotransferase (NylD1) catalyzes the reaction of 6-aminohexanoate to adipate semialdehyde using alpha-ketoglutarate, pyruvate, and glyoxylate as amino acceptors, generating glutamate, alanine, and glycine, respectively. The reaction requires pyridoxal phosphate (PLP) as a cofactor. For further metabolism, adipate semialdehyde dehydrogenase (NylE1) catalyzes the oxidative reaction of adipate semialdehyde to adipate using NADP+ as a cofactor |
752570 |
| 3.5.1.117 | more |
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 |
-, 730264 |
| 3.5.1.117 | more |
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 |
-, 730264, 734851 |
