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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

Reaction

N-(6-aminohexanoyl)-6-aminohexanoate
+
H2O
= 2 6-aminohexanoate

Synonyms

6-aminohexanoic acid oligomer hydrolase, EII, EII', Nylon oligomers degrading enzyme EII, Nylon oligomers degrading enzyme EII', nylon oligomer hydrolase, 6-aminohexanoate oligomer hydrolase, NylCA, NylCK, NylCP2, Hyb-24DN, nylon-oligomer degrading enzyme, NylB, 6-aminohexanoate-dimer hydrolase, N-(6-aminohexanoyl)-6-aminohexanoate amidohydrolase, 6-aminohexanoate dimer hydrolase, Ahx dimer hydrolase, Hyb-24

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.46 6-aminohexanoate-oligomer exohydrolase

Engineering

Engineering on EC 3.5.1.46 - 6-aminohexanoate-oligomer exohydrolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D181N
-
site-directed mutagenesis of EII, the mutant shows reduced activity compared to the wild-type enzyme
D181E
-
site-directed mutagenesis of EII, the mutant shows reduced activity compared to the wild-type enzyme
D181K
-
site-directed mutagenesis of EII, nearly inactive mutant
D181H
-
site-directed mutagenesis of EII, the mutant shows highly reduced activity compared to the wild-type enzyme
T3A/P4R/T5S/S8Q/D15G
T3A/P4R/T5S/S8Q/D15G/G181D/D370Y
-
site-directed mutagenesis, mutant Hyb24, by five amino acid replacement in EII' for residues of EII, plus 2 additional exchanges for EII residues leading to a 100fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate
T3A/P4R/T5S/S8Q/D15G/G181D
-
site-directed mutagenesis, mutant Hyb24, by five amino acid replacement in EII' for residues of EII, plus 2 additional exchanges for EII residues leading to a 10fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate
T3A/P4R/T5S/S8Q/D15G/D370Y
-
site-directed mutagenesis, mutant Hyb24, by five amino acid replacement in EII' for residues of EII, plus 2 additional exchanges for EII residues leading to a 10fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate
A61V/A253T/F264C/D370Y
-
site-directed mutagenesis, 10fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate
D181N
-
mutant with increased Km and decreased activity
D181E
-
mutant with increased Km and decreased activity
D181N
-
mutant with increased Km and decreased activity
-
D181E
-
mutant with increased Km and decreased activity
-
D181K
-
-
-
D181H
-
-
-
R187A
site-directed mutagenesis, the substitution in the parental Hyb-24DNY decreases the specific activity (initial reaction rate) of synthesis to 37% of the level of Hyb-24DNY
R187G
site-directed mutagenesis, the substitution in the parental Hyb-24DNY decreases the specific activity (initial reaction rate) of synthesis to 15% of the level of Hyb-24DNY
R187S
site-directed mutagenesis, the substitution in the parental Hyb-24DNY decreases the specific activity (initial reaction rate) of synthesis to 24% of the level of Hyb-24DNY
G181D/H266N
construction of NylB mutant enzyme Hyb-24DN, the activity in Hyb-24 is enhanced 150fold by the two substitutions, where Asp181-COO- stabilizes the substrate binding by electrostatic interactions with Ald-NH3+, and Asn266 cooperatively improves the electrostatic environment with Asp181
A61V/A124V/R187S/F264C/G291R/G338A/D370Y
site-directed mutagenesis
R187S/F264C/D370Y
site-directed mutagenesis, the substitutions also enhance the Ald-hydrolytic activity 80fold over the parental Hyb-24 enzyme. The directly evolved enzyme (Hyb-S4M94) possesses almost no Ald-synthetic activity, although it possesses high levels of the hydrolytic activity even in 90% t-butyl alcohol. In this mutant enzyme, the R187S/F264C substitutions stabilizes the binding at the N-terminal region of Ald, while D370Y substitution stabilizes the binding at the C-terminal region of Ald
additional information
construction of chimeric NylB/NylB' mutants Hyb-24DN and Hyb-24DNY. A NylB/NylB' hybrid enzyme Hyb-24 (NylB' containing T3A-P4R-T5S-S8Q-D15G substitutions) has about 0.5% of the NylB level of Ald-hydrolytic activity. Surface structure of the entrance of the catalytic cleft of the Hyb-24DNY and its mutant enzymes, wild-type and mutant kinetics, detailed overview