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Literature summary for 2.3.1.5 extracted from

  • Cloete, R.; Akurugu, W.A.; Werely, C.J.; van Helden, P.D.; Christoffels, A.
    Structural and functional effects of nucleotide variation on the human TB drug metabolizing enzyme arylamine N-acetyltransferase 1 (2017), J. Mol. Graph. Model., 75, 330-339 .
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
E264K single nucleotide variant, identified within a South African mixed ancestry population, substitution occupies less conformational clusters of folded states as compared to the wild-type and is destabilizing Homo sapiens
E264K single nucleotide variant, identified within a South African mixed ancestry population. Less thermodynamically stable protein structure is predicted Homo sapiens
N245I single nucleotide variant, identified within a South African mixed ancestry population. Thermodynamically stabilizing effect structure is predicted and affecting NAT1 protein function Homo sapiens
R242M single nucleotide variant, identified within a South African mixed ancestry population, displays a similar profile to the published variant, I263V (proposed fast acetylator), and the wild-type protein structure Homo sapiens
V231G single nucleotide variant, identified within a South African mixed ancestry population, substitution occupies less conformational clusters of folded states as compared to the wild-type and is destabilizing Homo sapiens
V231G single nucleotide variant, identified within a South African mixed ancestry population. Less thermodynamically stable protein structure and is predicted, and affecting NAT1 protein function Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P18440
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