ABCD1 p.Gln178Arg
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PMID: 17512009
[PubMed]
Negoro S et al: "Nylon-oligomer degrading enzyme/substrate complex: catalytic mechanism of 6-aminohexanoate-dimer hydrolase."
No.
Sentence
Comment
150
Although the large spatial distance should prevent Gln178-N from interacting with the substrate, replacement of Gln178 with Arg in the nylon-oligomer hydrolase significantly decreases the Ald-hydrolytic activity.
X
ABCD1 p.Gln178Arg 17512009:150:112
status: NEW151 Namely, D181N single substitution in EII-type protein (Hyb-2) decreases the Ald-hydrolytic activity to ca 5% of the parental EII level, while D181N/Q178R double substitutions possess a more drastic effect (0.25% of the EII level).37 Therefore, Gln178 may play a role in Ald-binding to the nylon-oligomer hydrolase.
X
ABCD1 p.Gln178Arg 17512009:151:148
status: NEW152 Although the large spatial distance should prevent Gln178-N from interacting with the substrate, replacement of Gln178 with Arg in the nylon-oligomer hydrolase significantly decreases the Ald-hydrolytic activity.
X
ABCD1 p.Gln178Arg 17512009:152:112
status: NEW153 Namely, D181N single substitution in EII-type protein (Hyb-2) decreases the Ald-hydrolytic activity to ca 5% of the parental EII level, while D181N/Q178R double substitutions possess a more drastic effect (0.25% of the EII level).37 Therefore, Gln178 may play a role in Ald-binding to the nylon-oligomer hydrolase.
X
ABCD1 p.Gln178Arg 17512009:153:148
status: NEW