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.
Appl Environ Microbiol
; 59(11): 3978-80, 1993 Nov.
Article
en En
| MEDLINE
| ID: mdl-8285701
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Flavobacterium
/
Amidohidrolasas
/
Genes Bacterianos
Idioma:
En
Revista:
Appl Environ Microbiol
Año:
1993
Tipo del documento:
Article
País de afiliación:
Japón
Pais de publicación:
Estados Unidos