Nylon oligomer degradation gene, nylC, on plasmid pOAD2 from a Flavobacterium strain encodes endo-type 6-aminohexanoate oligomer hydrolase: purification and characterization of the nylC gene product.
A new type of nylon oligomer degradation enzyme (EIII) was purified from an Escherichia coli clone harboring the EIII gene (nylC). This enzyme hydrolyzed the linear trimer, tetramer, and pentamer of 6-aminohexanoate by an endo-type reaction, and this specificity is different from that of the EI (nylA gene product) and EII (nylB gene product). Amino acid sequencing and sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified EIII demonstrated that the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267.
Kakudo
S
S
Department of Biotechnology, Osaka University, Japan.
Negoro
S
S
Urabe
I
I
Okada
H
H
D000581:Amidohydrolases / Q000235:genetics* / Q000302:isolation & purification; D000614:Aminocaproates; D015119:Aminocaproic Acid / Q000378:metabolism; D001673:Biodegradation, Environmental; D005417:Flavobacterium / Q000201:enzymology* / Q000235:genetics*; D005798:Genes, Bacterial; D009757:Nylons / Q000378:metabolism; D013379:Substrate Specificity
C026243:6-aminohexanoic acid cyclic dimer; D000614:Aminocaproates; D009757:Nylons; D000581:Amidohydrolases; C026250:6-aminohexanoate-dimer hydrolase; D015119:Aminocaproic Acid