EC Number   |
General Information |
Reference |
|---|
   3.5.1.46 | evolution |
6-aminohexanoate-dimer hydrolase (NylB) and NylB' carboxylesterase (88% homologous to NylB) are members of the penicillin-recognizing family of serine-reactive hydrolases. The NylB and NylB' utilize Ser112-Lys115-Tyr215 as catalytic triad, and catalyze the hydrolytic reaction of the Ahx-linear dimer (Ald) |
753567 |
| 3.5.1.46 | evolution |
Ahx dimer hydrolase (NylB), a member of the penicillin-recognizing family of serine-reactive hydrolases |
752570 |
| 3.5.1.46 | malfunction |
the yield of this reverse reaction in 90% t-butyl alcohol vaies drastically when enzyme mutants with substitutions of several amino acids located at the entrance of the catalytic cleft are used |
753567 |
| 3.5.1.46 | 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-oxoglutarate, pyruvate, and glyoxylate as amino acceptors, generating glutamate, alanine, and glycine, respectively. The reaction requires pyridoxal phosphate 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 |
| 3.5.1.46 | more |
enzyme Ahx dimer hydrolase hydrolyzes the Ahx oligomers by an exo-type mechanism |
752570 |
| 3.5.1.46 | more |
hydration effects on enzyme-substrate complex of nylon oligomer hydrolase, inter-fragment interaction energy study by the fragment molecular orbital method, overview. Interactions between the substrate, 6-aminohexanoate linear dimer (ALD), and the amino acid residues, such as Asp181, Ser112, and Ile 345, which are regarded as important for enzyme-substrate complex formation by NylB.The direct interaction between ALD and NylB is weakens by hydration, because water molecules cause charge translation or polarisation of ALD or each amino acid residue. But including the interaction energy between ALD and water molecules greatly stabilises this complex. These results indicate the importance of the hydration effects in enzyme-substrate complex formation, quantitative analysis |
754782 |
| 3.5.1.46 | more |
residues Ser112, Lys115, and Tyr215 form the catalytic triad of enzyme NylB |
753567 |
