EC Number   |
General Information |
Reference |
|---|
   2.3.1.5 | physiological function |
following NAT1 knockdown with shRNA, acetylation of p-aminobenzoylglutamate is significantly decreased, while there are no changes in intracellular p-aminobenzoylglutamate or the components of the SAM cycle. The flux of homocysteine in the medium is different following NAT1 knockdown after the methionine content is exhausted. NAT1 knockdown inhibits the methionine salvage pathway in HT-29 cells but not in HeLa or MDA-MB-436 cells |
756019 |
| 2.3.1.5 | physiological function |
increasing acetylation by introduction of the human NAT1 transgene is protective against sporadic dilantin-induced orofacial clefting defects in the mouse A/J strain |
705823 |
| 2.3.1.5 | physiological function |
isoform NAT1 is strongly expressed in oestrogen receptor-positive breast cancer and may contribute to folate and acetyl CoA homeostasis |
735871 |
| 2.3.1.5 | physiological function |
knock-down of enzyme by lentiviral shRNA reduces the invasion potential of MDA-MB-231 cells. Enzymic activity may be important in breast cancer growth and metastasis |
702102 |
| 2.3.1.5 | physiological function |
knockdown of N-acetyltransferase by siRNA results in downregulation of thymidylate synthase mRNA expression and induced apoptosis. N-acetyltransferase overexpression facilitates cell proliferation independent of the presence of 5-fluorouracil |
701721 |
| 2.3.1.5 | physiological function |
knockout of NAT2 significantly decreases teratogen-induced orofacial clefting in the A/J strain, but not in the C57BL/6J strain |
705823 |
| 2.3.1.5 | physiological function |
loss of NAT1 in in MDA-MB-231, HT-29 and HeLa cells increases adherence to collagen but migration of cells is unaffected. NAT1 deletion decreases invasion and induces changes to cell morphology. These effects are independent of matrix metalloproteinases but are related to integrin ITGalphaV expression |
756372 |
| 2.3.1.5 | physiological function |
N-acetylation of 4-aminobenzoate varies markedly among the peripheral mononuclear blood cells of donors, but correlate very significantly with levels of NAT1 transcripts. Allelic variation NAT1*4 subjects show significantly higher apparent 4-aminobenzoate Vmax of 71.3 versus the NAT1*14B subjects apparent Vmax of 58.5 nmoles N-acetyl 4-aminobenzoate/24 h/million cells. Levels of 4-aminobenzoate N-acetylation activity at each concentration of substrate evaluated also significantly correlate with NAT1 mRNA levels for all samples |
755913 |
| 2.3.1.5 | physiological function |
NAT1 deletion decreases oxidative phosphorylation with a significant loss in respiratory reserve capacity in both MDA-MB-231 and HT-29 cell lines. There is a decrease in glycolysis without a change in glucose uptake. The changes in mitochondrial function are due to a decrease in pyruvate dehydrogenase activity. Pyruvate dehydrogenase activity is attenuated either by an increase in phosphorylation or a decrease in total protein expression |
756928 |
| 2.3.1.5 | physiological function |
NAT1-specific shRNA reduces NAT1 activity in vitro by 39%, increases endogenous acetyl coenzyme A levels by 35%, and reduces anchorage-independent growth (7fold) without significant effects on cell morphology, growth rates, anchorage-dependent colony formation, or invasiveness. 12fold overexpression of NAT1 activity does not significantly affect anchorage-dependent cell growth, anchorage-independent cell growth, and relative invasiveness |
757645 |
