Difference between revisions of "YEL066W"
SGDwikiBot (talk | contribs) (Automated import of articles) |
SGDwikiBot (talk | contribs) (Automated import of articles) |
||
| Line 1: | Line 1: | ||
<!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN--> | <!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN--> | ||
{{PageTop}} | {{PageTop}} | ||
| + | <protect> | ||
{|{{Prettytable}} align = 'right' width = '200px' | {|{{Prettytable}} align = 'right' width = '200px' | ||
|- | |- | ||
| Line 13: | Line 14: | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
|nowrap| Chr V:26667..27206 | |nowrap| Chr V:26667..27206 | ||
| − | |||
| − | |||
|} | |} | ||
<br> | <br> | ||
| Line 23: | Line 22: | ||
<br> | <br> | ||
<br> | <br> | ||
| − | + | <br> | |
| + | </protect> | ||
__TOC__ | __TOC__ | ||
==Community Commentary== | ==Community Commentary== | ||
{{CommentaryHelp}} | {{CommentaryHelp}} | ||
| + | |||
| + | <protect> | ||
==References== | ==References== | ||
<!-- REFERENCES ARE AUTOMATICALLY GENERATED. PLEASE DON'T EDIT THIS SECTION--> | <!-- REFERENCES ARE AUTOMATICALLY GENERATED. PLEASE DON'T EDIT THIS SECTION--> | ||
{{RefHelp}} | {{RefHelp}} | ||
| + | </protect> | ||
Revision as of 08:17, 30 January 2007
Share your knowledge...Edit this entry! <protect>
| Systematic name | YEL066W |
| Gene name | HPA3 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr V:26667..27206 |
Description of YEL066W: D-Amino acid N-acetyltransferase, catalyzes N-acetylation of D-amino acids through ordered bi-bi mechanism in which acetyl-CoA is first substrate bound and CoA is last product liberated; similar to Hpa2p, acetylates histones weakly in vitro[1][2]
</protect>
Contents
Community Commentary
About Community Commentary. Please share your knowledge!
<protect>
References
See Help:References on how to add references
- ↑ Yow GY, et al. (2004) D-amino acid N-acetyltransferase of Saccharomyces cerevisiae: a close homologue of histone acetyltransferase Hpa2p acting exclusively on free D-amino acids. Arch Microbiol 182(5):396-403 SGD PMID 15375647
- ↑ Angus-Hill ML, et al. (1999) Crystal structure of the histone acetyltransferase Hpa2: A tetrameric member of the Gcn5-related N-acetyltransferase superfamily. J Mol Biol 294(5):1311-25 SGD PMID 10600387
See Help:Categories on how to add the wiki page for this gene to a Category </protect>
