1e2t
From Proteopedia
(New page: 200px<br /> <applet load="1e2t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e2t, resolution 2.8Å" /> '''ARYLAMINE N-ACETYLTR...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1E2T is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.118 2.3.1.118]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E2T OCA]]. | + | 1E2T is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]]. Active as [[http://en.wikipedia.org/wiki/N-hydroxyarylamine_O-acetyltransferase N-hydroxyarylamine O-acetyltransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.118 2.3.1.118]]. Structure known Active Sites: AS1, AS2, AS3, AS4, AS5, AS6, AS7 and AS8. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E2T OCA]]. |
==Reference== | ==Reference== | ||
Structure of arylamine N-acetyltransferase reveals a catalytic triad., Sinclair JC, Sandy J, Delgoda R, Sim E, Noble ME, Nat Struct Biol. 2000 Jul;7(7):560-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10876241 10876241] | Structure of arylamine N-acetyltransferase reveals a catalytic triad., Sinclair JC, Sandy J, Delgoda R, Sim E, Noble ME, Nat Struct Biol. 2000 Jul;7(7):560-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10876241 10876241] | ||
| + | [[Category: N-hydroxyarylamine O-acetyltransferase]] | ||
[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:35:59 2007'' |
Revision as of 10:31, 30 October 2007
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ARYLAMINE N-ACETYLTRANSFERASE (NAT) FROM SALMONELLA TYPHIMURIUM
Overview
Enzymes of the arylamine N-acetyltransferase (NAT) family are found in, species ranging from Escherichia coli to humans. In humans they are known, to be responsible for the acetylation of a number of arylamine and, hydrazine drugs, and they are strongly linked to the carcinogenic, potentiation of certain foreign substances. In prokaryotes their substrate, specificities may vary and members of the gene family have been linked to, pathways including amide synthesis during rifamycin production. Here we, report the crystal structure at 2.8 A resolution of a representative, member of this family from Salmonella typhimurium in the presence and, absence of a covalently bound product analog. The structure reveals, surprising mechanistic information including the presence of a Cys-His-Asp, ... [(full description)]
About this Structure
1E2T is a [Single protein] structure of sequence from [Salmonella typhimurium]. Active as [N-hydroxyarylamine O-acetyltransferase], with EC number [2.3.1.118]. Structure known Active Sites: AS1, AS2, AS3, AS4, AS5, AS6, AS7 and AS8. Full crystallographic information is available from [OCA].
Reference
Structure of arylamine N-acetyltransferase reveals a catalytic triad., Sinclair JC, Sandy J, Delgoda R, Sim E, Noble ME, Nat Struct Biol. 2000 Jul;7(7):560-4. PMID:10876241
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