Arylamine N-acetyltransferase
From Proteopedia
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| - | + | <StructureSection load='2pqt' size='350' side='right' caption='Human arylamine N-acetyltransferase 1 with active site Cys intermediate complex with Cl- (green) (PDB code [[2pqt]])' scene='48/486362/Cv/1'> | |
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== Function == | == Function == | ||
| - | '''Arylamine N-acetyltransferase''' (NAT) catalyzes the transfer of an acetyl group from acetyl-CoA to an arylamine. | + | '''Arylamine N-acetyltransferase''' (NAT) catalyzes the transfer of an acetyl group from acetyl-CoA to an arylamine. Human NAT have 2 polymorphs with different substrate specificities. '''NAT1''' acetylates p-aminisalycilates while '''NAT2''' acetylates hydralazine. |
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| + | == Disease == | ||
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| + | Human NAT1 is overexpressed in some kinds of breast cancer. | ||
== Relevance == | == Relevance == | ||
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Acetylation is a major route of biotransformation for many arylamines and hydrazine drugs and known carcinogens like cigarette smoke. The levels of NAT in the body has important consequences with regard to an individual’s susceptibility to certain drug-induced toxicities and cancer. | Acetylation is a major route of biotransformation for many arylamines and hydrazine drugs and known carcinogens like cigarette smoke. The levels of NAT in the body has important consequences with regard to an individual’s susceptibility to certain drug-induced toxicities and cancer. | ||
| - | == | + | == Structural highlights == |
| - | + | NAT acetylates using a <scene name='48/486362/Cv/4'>catalytic Cys-His-Asp triad</scene> (magenta). <ref>PMID:17656365</ref> TYX is colored in salmon. | |
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| - | + | ==3D structures of arylamine N-acetyltransferase== | |
| - | + | [[Arylamine N-acetyltransferase 3D structures]] | |
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| - | + | </StructureSection> | |
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| - | + | == References == | |
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ Wu H, Dombrovsky L, Tempel W, Martin F, Loppnau P, Goodfellow GH, Grant DM, Plotnikov AN. Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases. J Biol Chem. 2007 Oct 12;282(41):30189-97. Epub 2007 Jul 26. PMID:17656365 doi:10.1074/jbc.M704138200
