Abstract
Humans possess twoN-acetyltransferase isozymes (NAT1 and NAT2). We cloned and sequenced a novelNAT1allele (Genbank HSU 80835) that contained nucleotide substitutions at -344 (C→T), -40 (A→T), 445 [G→A(Val→Ile)], 459 [G→A(silent)], 640 [T→G(Ser→Ala)], a 9 base pair deletion between nucleotides 1065 and 1090, and 1095 (C→A). The novelNAT1allele which we have designatedNAT1*17is similar toNAT1*11except for a G445A substitution (Val149→Ile) in theNAT1coding region. The G445A (Val149→Ile) substitution yielded no significant changes in levels of immunoreactivity, as detected by Western blot, nor in intrinsic stability of the recombinant N-acetyltransferase protein. However, the G445A (Val149→Ile) substitution yielded expression of recombinant NAT1 protein that catalyzed theN-acetylation of aromatic amines and theO- andN,O-acetylation of theirN-hydroxylated metabolites at rates up to 2-fold higher than wild-type recombinant human NAT1.
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