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Literature summary for 3.5.1.117 extracted from

  • Kakudo, S.; Negoro, S.; Urabe, I.; Okada, H.
    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 (1993), Appl. Environ. Microbiol., 59, 3978-3980.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.117

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
9000
-
 x * 31000 + x * 9000, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, SDS-PAGE Flavobacterium sp.
9513
-
 x * 27408 + x * 9513, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, calculation from nucleotide sequence Flavobacterium sp.
27408
-
 x * 27408 + x * 9513, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, calculation from nucleotide sequence Flavobacterium sp.
31000
-
 x * 31000 + x * 9000, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, SDS-PAGE Flavobacterium sp.

Organism

Organism UniProt Comment Textmining
Flavobacterium sp. Q79F77
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Flavobacterium sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3
-
 pH 7.2, 30°C Flavobacterium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information negligible activity with N-(6-aminohexanoyl)-6-aminohexanoate and N-(6-aminohexanoyl)-N-(6-aminohexanoyl)-6-aminohexanoate and the cyclic dimer 1,8-diazacyclotetradecane-2,9-dione Flavobacterium sp. ?
-
 ?
N-(6-aminohexanoyl)-N-(6-aminohexanoyl)-N-(6-aminohexanoyl)-6-aminohexanoate + H2O endo-type reaction Flavobacterium sp. N-(6-aminohexanoyl)-N-(6-aminohexanoyl)-6-aminohexanoate + N-(6-aminohexanoyl)-N-(6-aminohexanoate)-6-aminohexanoate
-
 ?
N-(6-aminohexanoyl)-N-(6-aminohexanoyl)-N-(6-aminohexanoyl)-N-(6-aminohexanoate)-6-aminohexanoate + H2O endo-type reaction Flavobacterium sp. N-(6-aminohexanoyl)-N-(6-aminohexanoyl)-6-aminohexanoate + N-(6-aminohexanoyl)-6-aminohexanoate
-
 ?
nylon oligomer + H2O endo-type reaction. Linear oligomers of 6-aminohexanoate such as the tetramer and the pentamer are initially produced and subsequently converted to smaller oligomers such as the dimer. The enzyme predominantly cleaves amide bonds located at the second and third positions from the carbobenzoxy group. This enzyme favors a longer chain of linear oligomer digesting the internal amide bonds preferentially but has no activity toward N-(6-aminohexanoyl)-6-aminohexanoate or 6-aminohexanoate cyclic dimer Flavobacterium sp. ?
-
 ?

Subunits

Subunits Comment Organism
? x * 27408 + x * 9513, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, calculation from nucleotide sequence Flavobacterium sp.
? x * 31000 + x * 9000, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, SDS-PAGE Flavobacterium sp.

Synonyms

Synonyms Comment Organism
NylC
-
 Flavobacterium sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Flavobacterium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Flavobacterium sp.