3.5.1.46: 6-aminohexanoate-oligomer exohydrolase
This is an abbreviated version!
For detailed information about 6-aminohexanoate-oligomer exohydrolase, go to the full flat file.
Word Map on EC 3.5.1.46
-
3.5.1.46
-
flavobacterium
-
arthrobacter
-
nylon-6
-
amide
-
beta-lactamase
-
carboxylesterase
-
esterase
-
esterolytic
-
hydrolases
-
vapour-diffusion
-
tetrahedral
-
penicillin-recognizing
-
man-made
-
sitting-drop
-
compendium
- 3.5.1.46
- flavobacterium
- arthrobacter
- nylon-6
- amide
- beta-lactamase
- carboxylesterase
- esterase
-
esterolytic
- hydrolases
-
vapour-diffusion
-
tetrahedral
-
penicillin-recognizing
-
man-made
-
sitting-drop
-
compendium
Reaction
Synonyms
6-aminohexanoate dimer hydrolase, 6-aminohexanoate oligomer hydrolase, 6-aminohexanoate-dimer hydrolase, 6-aminohexanoic acid oligomer hydrolase, Ahx dimer hydrolase, EII, EII', Hyb-24, Hyb-24DN, N-(6-aminohexanoyl)-6-aminohexanoate amidohydrolase, NylB, NylCA, NylCK, NylCP2, nylon oligomer hydrolase, Nylon oligomers degrading enzyme EII, Nylon oligomers degrading enzyme EII', nylon-oligomer degrading enzyme
ECTree
3.5.1.46 6-aminohexanoate-oligomer exohydrolaseAdvanced search results
results (
results (General Information
General Information on EC 3.5.1.46 - 6-aminohexanoate-oligomer exohydrolase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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
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
additional information
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)
evolution
Ahx dimer hydrolase (NylB), a member of the penicillin-recognizing family of serine-reactive hydrolases
additional information
enzyme Ahx dimer hydrolase hydrolyzes the Ahx oligomers by an exo-type mechanism
additional information
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
additional information
residues Ser112, Lys115, and Tyr215 form the catalytic triad of enzyme NylB
