Function
6-aminohexanoate-dimer hydrolase (AHDH) catalyzes the conversion of N-(6-aminohexanoyl)-6-aminohexanoate to 6-aminohexanoate monomers. AHDH is part of the xenobiotic degradation[1]. It belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides[2].
Relevance
AHDH degrades the industrial byproduct nylon 6.
Structural highlights
6-aminohexanoate binding site (PDB code 2zm9).[3] Water molecules are shown as red spheres.
3D structures of 6-aminohexanoate-dimer hydrolase
6-aminohexanoate-dimer hydrolase 3D structures
- ↑ Negoro S, Shibata N, Tanaka Y, Yasuhira K, Shibata H, Hashimoto H, Lee YH, Oshima S, Santa R, Oshima S, Mochiji K, Goto Y, Ikegami T, Nagai K, Kato D, Takeo M, Higuchi Y. Three-dimensional structure of nylon hydrolase and mechanism of nylon-6 hydrolysis. J Biol Chem. 2012 Feb 10;287(7):5079-90. doi: 10.1074/jbc.M111.321992. Epub 2011 , Dec 19. PMID:22187439 doi:https://dx.doi.org/10.1074/jbc.M111.321992
- ↑ Kinoshita S, Terada T, Taniguchi T, Takene Y, Masuda S, Matsunaga N, Okada H. Purification and characterization of 6-aminohexanoic-acid-oligomer hydrolase of Flavobacterium sp. Ki72. Eur J Biochem. 1981 Jun 1;116(3):547-51. PMID:7262074 doi:10.1111/j.1432-1033.1981.tb05371.x
- ↑ Ohki T, Shibata N, Higuchi Y, Kawashima Y, Takeo M, Kato D, Negoro S. Two alternative modes for optimizing nylon-6 byproduct hydrolytic activity from a carboxylesterase with a beta-lactamase fold: X-ray crystallographic analysis of directly evolved 6-aminohexanoate-dimer hydrolase. Protein Sci. 2009 Aug;18(8):1662-73. PMID:19521995 doi:10.1002/pro.185
