Matches in SemOpenAlex for { <https://semopenalex.org/work/W2043203418> ?p ?o ?g. }
- W2043203418 endingPage "510" @default.
- W2043203418 startingPage "479" @default.
- W2043203418 abstract "Arylamine N-acetyltransferases (NATs) are cytosolic conjugating enzymes which transfer an acetyl group from acetylCoenzyme A to a xenobiotic acceptor substrate. The enzyme has an active site cysteine as part of a catalytic triad with histidine and aspartate. NATs have had an important role in pharmacogenetics. Polymorphism in acetylation (and inactivation) of the anti-tubercular agent isoniazid resides in human NAT2, one of two polymorphic human NATs. In humans there is also a third pseudogene and in rodents there are three isozymes. Comparison of human and rodent NAT enzymes and their genes is aiding our understanding of the roles of the individual isoenzymes. This may have clinical importance since human NAT1 is overexpressed in a sub-population of breast cancers and control of expression of the NAT genes is ripe for investigation. The mammalian NAT enzymes are involved in metabolism of drugs and carcinogens but there is growing evidence, including from transgenic mice, that human NAT1 has an endogenous role in folate degradation. Structural studies and intracellular tracking of polymorphic NAT variants, is contributing to appreciation of how individual mutations result in loss of NAT activity. Genome analyses have identified NAT homologues in bacteria including Mycobacterium tuberculosis, in which the NAT enzyme metabolises inactivation of isoniazid. More intriguingly, deletion of the nat gene in mycobacteria, leads to deficits in cell wall synthesis. Structural comparisons of NATs from prokaryotes and eukaryotes, particularly in relation to CoA binding, provide a platform for understanding how the unique NAT protein fold may lend itself to a wide range of functions." @default.
- W2043203418 created "2016-06-24" @default.
- W2043203418 creator A5009319585 @default.
- W2043203418 creator A5054888023 @default.
- W2043203418 creator A5071196257 @default.
- W2043203418 date "2008-01-01" @default.
- W2043203418 modified "2023-09-30" @default.
- W2043203418 title "Arylamine N-acetyltransferases: From Structure to Function" @default.
- W2043203418 cites W1491175805 @default.
- W2043203418 cites W1516667778 @default.
- W2043203418 cites W1579627745 @default.
- W2043203418 cites W1600133349 @default.
- W2043203418 cites W1607267312 @default.
- W2043203418 cites W1757108108 @default.
- W2043203418 cites W1782287000 @default.
- W2043203418 cites W1952488157 @default.
- W2043203418 cites W1967856083 @default.
- W2043203418 cites W1969105152 @default.
- W2043203418 cites W1969336855 @default.
- W2043203418 cites W1973088446 @default.
- W2043203418 cites W1976173969 @default.
- W2043203418 cites W1977918192 @default.
- W2043203418 cites W1978365776 @default.
- W2043203418 cites W1980335231 @default.
- W2043203418 cites W1980571658 @default.
- W2043203418 cites W1982167929 @default.
- W2043203418 cites W1986301467 @default.
- W2043203418 cites W1988146888 @default.
- W2043203418 cites W1988606561 @default.
- W2043203418 cites W1988855705 @default.
- W2043203418 cites W1989498124 @default.
- W2043203418 cites W1989632769 @default.
- W2043203418 cites W1990449229 @default.
- W2043203418 cites W1996427775 @default.
- W2043203418 cites W1996770386 @default.
- W2043203418 cites W1998790265 @default.
- W2043203418 cites W1999549596 @default.
- W2043203418 cites W2000881627 @default.
- W2043203418 cites W2002280541 @default.
- W2043203418 cites W2004373161 @default.
- W2043203418 cites W2007366149 @default.
- W2043203418 cites W2009366846 @default.
- W2043203418 cites W2016064391 @default.
- W2043203418 cites W2019329593 @default.
- W2043203418 cites W2021867944 @default.
- W2043203418 cites W2022928028 @default.
- W2043203418 cites W2039408159 @default.
- W2043203418 cites W2042897001 @default.
- W2043203418 cites W2043512288 @default.
- W2043203418 cites W2044312503 @default.
- W2043203418 cites W2045492912 @default.
- W2043203418 cites W2047480828 @default.
- W2043203418 cites W2048005096 @default.
- W2043203418 cites W2049600834 @default.
- W2043203418 cites W2052773860 @default.
- W2043203418 cites W2052843890 @default.
- W2043203418 cites W2053143978 @default.
- W2043203418 cites W2054454959 @default.
- W2043203418 cites W2054608792 @default.
- W2043203418 cites W2055266236 @default.
- W2043203418 cites W2055786949 @default.
- W2043203418 cites W2058922431 @default.
- W2043203418 cites W2062626341 @default.
- W2043203418 cites W2063360787 @default.
- W2043203418 cites W2064899351 @default.
- W2043203418 cites W2066959869 @default.
- W2043203418 cites W2068586920 @default.
- W2043203418 cites W2069455052 @default.
- W2043203418 cites W2069890113 @default.
- W2043203418 cites W2070669906 @default.
- W2043203418 cites W2070858213 @default.
- W2043203418 cites W2075470465 @default.
- W2043203418 cites W2077249120 @default.
- W2043203418 cites W2077535572 @default.
- W2043203418 cites W2078424288 @default.
- W2043203418 cites W2078433308 @default.
- W2043203418 cites W2082802949 @default.
- W2043203418 cites W2082840313 @default.
- W2043203418 cites W2084185692 @default.
- W2043203418 cites W2085231301 @default.
- W2043203418 cites W2088852867 @default.
- W2043203418 cites W2092128596 @default.
- W2043203418 cites W2093363647 @default.
- W2043203418 cites W2093380647 @default.
- W2043203418 cites W2095038216 @default.
- W2043203418 cites W2096358451 @default.
- W2043203418 cites W2097193332 @default.
- W2043203418 cites W2099892638 @default.
- W2043203418 cites W2100289966 @default.
- W2043203418 cites W2100357455 @default.
- W2043203418 cites W2102821513 @default.
- W2043203418 cites W2103808653 @default.
- W2043203418 cites W2104551057 @default.
- W2043203418 cites W2106321527 @default.
- W2043203418 cites W2110125737 @default.
- W2043203418 cites W2111780976 @default.
- W2043203418 cites W2113120738 @default.
- W2043203418 cites W2114245165 @default.