ABCMdb

PMID: 17512009

Negoro S, Ohki T, Shibata N, Sasa K, Hayashi H, Nakano H, Yasuhira K, Kato D, Takeo M, Higuchi Y
Nylon-oligomer degrading enzyme/substrate complex: catalytic mechanism of 6-aminohexanoate-dimer hydrolase.
J Mol Biol. 2007 Jun 29;370(1):142-56. Epub 2007 Apr 24., [PubMed]

Sentences

No. Mutations Sentence Comment

150 ABCD1 p.Gln178Arg 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. Login to comment 151 ABCD1 p.Gln178Arg 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. Login to comment 152 ABCD1 p.Gln178Arg 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. Login to comment 153 ABCD1 p.Gln178Arg 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. Login to comment