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. 1993 Nov;59(11):3978–3980. doi: 10.1128/aem.59.11.3978-3980.1993

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.

S Kakudo 1, S Negoro 1, I Urabe 1, H Okada 1
PMCID: PMC182563  PMID: 8285701

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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