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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== Structural highlights == | == Structural highlights == | ||
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| + | 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. | ||
==3D structures of arylamine N-acetyltransferase== | ==3D structures of arylamine N-acetyltransferase== | ||
| + | [[Arylamine N-acetyltransferase 3D structures]] | ||
| - | + | </StructureSection> | |
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| - | + | == References == | |
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[[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
