X-ray crystallographic analysis of the 6-aminohexanoate cyclic dimer hydrolase catalytic mechanism and evolution of an enzyme responsible for nylon-6 byproduct …

…, G Mongami, Y Uedo, Y Atsumi, Y Kawashima…

Index: Yasuhira, Kengo; Shibata, Naoki; Mongami, Go; Uedo, Yuki; Atsumi, Yu; Kawashima, Yasuyuki; Hibino, Atsushi; Tanaka, Yusuke; Lee, Young-Ho; Kato, Dai-Ichiro; Takeo, Masahiro; Higuchi, Yoshiki; Negoro, Seiji Journal of Biological Chemistry, 2010 , vol. 285, # 2 p. 1239 - 1248

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Citation Number: 21

Abstract

Abstract We performed x-ray crystallographic analyses of the 6-aminohexanoate cyclic dimer (Acd) hydrolase (NylA) from Arthrobacter sp., an enzyme responsible for the degradation of the nylon-6 industry byproduct. The fold adopted by the 472-amino acid polypeptide generated a compact mixed α/β fold, typically found in the amidase signature superfamily; this fold was especially similar to the fold of glutamyl-tRNA Gln ...