Difference between revisions of "YEL066W"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl? | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000792 YEL066W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HPA3 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HPA3 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
|nowrap| Chr V:26667..27206 | |nowrap| Chr V:26667..27206 | ||
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000000792 | ||
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<br> | <br> | ||
| − | '''Description of | + | '''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<ref name='S000079786'>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 {{SGDpaper|S000079786}} PMID 15375647</ref><ref name='S000056329'>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 |
{{SGDpaper|S000056329}} PMID 10600387</ref> | {{SGDpaper|S000056329}} PMID 10600387</ref> | ||
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J Biol Chem 278(5):3265-74</ref> | J Biol Chem 278(5):3265-74</ref> | ||
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<protect> | <protect> | ||
Revision as of 08:45, 27 February 2007
Share your knowledge...Edit this entry! <protect>
| Systematic name | YEL066W |
| Gene name | HPA3 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr V:26667..27206 |
| Primary SGDID | S000000792 |
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]
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References
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- ↑ 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
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