Difference between revisions of "YEL066W"
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| − | '''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=' | + | '''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| | + | {{SGDpaper|S000056329}} PMID 10600387</ref> |
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Revision as of 14:05, 16 January 2009
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| 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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