Literature summary extracted from
Ohki, T.; Wakitani, Y.; Takeo, M.; Yasuhira, K.; Shibata, N.; Higuchi, Y.; Negoro, S.
Mutational analysis of 6-aminohexanoate-dimer hydrolase: relationship between nylon oligomer hydrolytic and esterolytic activities (2006), FEBS Lett., 580, 5054-5058.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.5.1.46 |
nylB24 gene, expression of the His-tagged EII-EII'-hybrid Hyb24 in Escherichia coli strain KP3998 |
Arthrobacter sp. |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.5.1.46 |
A61V/A253T/F264C/D370Y |
site-directed mutagenesis, 10fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate |
Arthrobacter sp. |
3.5.1.46 |
T3A/P4R/T5S/S8Q/D15G |
site-directed mutagenesis, construction of a hybrid of isozymes EII and EII', termed Hyb24, by five amino acid replacement in EII', the mutant shows the same activity as EII' |
Arthrobacter sp. |
3.5.1.46 |
T3A/P4R/T5S/S8Q/D15G/D370Y |
site-directed mutagenesis, mutant Hyb24, by five amino acid replacement in EII' for residues of EII, plus 2 additional exchanges for EII residues leading to a 10fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate |
Arthrobacter sp. |
3.5.1.46 |
T3A/P4R/T5S/S8Q/D15G/G181D |
site-directed mutagenesis, mutant Hyb24, by five amino acid replacement in EII' for residues of EII, plus 2 additional exchanges for EII residues leading to a 10fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate |
Arthrobacter sp. |
3.5.1.46 |
T3A/P4R/T5S/S8Q/D15G/G181D/D370Y |
site-directed mutagenesis, mutant Hyb24, by five amino acid replacement in EII' for residues of EII, plus 2 additional exchanges for EII residues leading to a 100fold increased activity with N-(6-aminohexanoyl)-6-aminohexanoate |
Arthrobacter sp. |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
3.5.1.46 |
N-(6-aminohexanoyl)-6-aminohexanoate + H2O |
Arthrobacter sp. |
the enzyme is responsible for the degradation of nylon-6 industrial production by-products |
6-aminohexanoate |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.5.1.46 |
Arthrobacter sp. |
- |
formerly Flavobacterium sp., strain K172, enzyme form EII and cryptic enzyme form EII' |
- |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
3.5.1.46 |
N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate |
structure-function relationship, residues 370 and 181 are imporatant for enzyme activity |
Arthrobacter sp. |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.5.1.46 |
N-(6-aminohexanoyl)-6-aminohexanoate + H2O |
the enzyme is responsible for the degradation of nylon-6 industrial production by-products |
Arthrobacter sp. |
6-aminohexanoate |
- |
? |
|
3.5.1.46 |
N-(6-aminohexanoyl)-6-aminohexanoate + H2O |
the enzyme hydrolyzes the linear dimer substrate |
Arthrobacter sp. |
6-aminohexanoate |
- |
? |
|