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TitleX-ray crystallographic analysis of the 6-aminohexanoate cyclic dimer hydrolase: catalytic mechanism and evolution of an enzyme responsible for nylon-6 byproduct degradation
Journal, issue, pagesJ. Biol. Chem., Vol. 285, Page 1239-1248, Year 2010
Publish dateMay 26, 2009 (structure data deposition date)
AuthorsYasuhira, K. / Shibata, N. / Mongami, G. / Uedo, Y. / Atsumi, Y. / Kawashima, Y. / Hibino, A. / Tanaka, Y. / Lee, Y.-H. / Kato, D. ...Yasuhira, K. / Shibata, N. / Mongami, G. / Uedo, Y. / Atsumi, Y. / Kawashima, Y. / Hibino, A. / Tanaka, Y. / Lee, Y.-H. / Kato, D. / Takeo, M. / Higuchi, Y. / Negoro, S.
External linksJ. Biol. Chem. / PubMed:19889645
MethodsX-ray diffraction
Resolution1.8 - 1.9 Å
Structure data

PDB-3a2p:
Structure of 6-aminohexanoate cyclic dimer hydrolase
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3a2q:
Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-ACA:
6-AMINOHEXANOIC ACID / inhibitor*YM

Source
  • arthrobacter sp. (bacteria)
KeywordsHYDROLASE / alpha/beta fold / Nylon degradation

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