Cloned (Comment) | Organism |
---|---|
isozyme NAT2, expression in Escherichia coli strain DJ2002 | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
E8G | site-directed mutagenesis, the NAT2 mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
F192Y | site-directed mutagenesis, the NAT2 mutant shows highly reduced activity compared to the wild-type enzyme | Homo sapiens |
H43R | site-directed mutagenesis, the NAT2 mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
I32V | site-directed mutagenesis, the NAT2 mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
K13R | site-directed mutagenesis, the NAT2 mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
K141E | site-directed mutagenesis, the NAT2 mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
L239F | site-directed mutagenesis, the NAT2 mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
L69P | site-directed mutagenesis, the NAT2 mutant shows highly reduced activity compared to the wild-type enzyme | Homo sapiens |
L74P | site-directed mutagenesis, the NAT2 mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
additional information | NAT2 random mutagenesis, developement of a system in which the activation of mutagens by recombinant human NAT 2, expressed in Escherichia coli, can be detected by the appearance of LacZ revertants, screening for variants of the human NAT2 sequence with altered activity, detailed overview | Homo sapiens |
Q133R | site-directed mutagenesis, the NAT2 mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
S102C | site-directed mutagenesis, the NAT2 mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
T250P | site-directed mutagenesis, the NAT2 mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
Y190C | site-directed mutagenesis, the NAT2 mutant shows highly reduced activity compared to the wild-type enzyme | Homo sapiens |
Y190F | site-directed mutagenesis, the NAT2 mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + 2-aminofluorene | Homo sapiens | - |
CoA + 2-acetylaminofluorene | - |
? | |
additional information | Homo sapiens | NAT plays a key role in the metabolic activation of aromatic amine and nitroaromatic mutagens to electrophilic reactive intermediates | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P11245 | isozyme NAT2; isozyme NAT2 | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
activity of recombinant wild-type and mutant NAT2, overview | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + 2-aminofluorene | - |
Homo sapiens | CoA + 2-acetylaminofluorene | - |
? | |
acetyl-CoA + 2-aminofluorene | interactions and substrate binding structure, overview | Homo sapiens | CoA + 2-acetylaminofluorene | - |
? | |
additional information | NAT plays a key role in the metabolic activation of aromatic amine and nitroaromatic mutagens to electrophilic reactive intermediates | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | modeling and analysis of the three-dimensional structures of human NAT enzymes, overview, sequence and structure comparisons, NAT2 model structure possesses three structural domains | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
NAT | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
acetyl-CoA | - |
Homo sapiens |