d-Amino acid-N-acetyltransferase of Saccharomyces cerevisiae: a close homologue of histone acetyltransferase Hpa2p acting exclusively on free d-amino acids
| Autor: | Tohru Yoshimura, Takuma Uo, Nobuyoshi Esaki, Geok Yong Yow |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Molecular Sequence Data Saccharomyces cerevisiae Amino-Acid N-Acetyltransferase SAP30 Biochemistry Microbiology Substrate Specificity Acetyltransferases Escherichia coli Genetics Amino Acid Sequence Histone octamer Amino Acids Molecular Biology Histone Acetyltransferases chemistry.chemical_classification biology HDAC9 Sequence Analysis DNA General Medicine Histone acetyltransferase biology.organism_classification Recombinant Proteins Amino acid Kinetics chemistry Histone methyltransferase Acetyltransferase biology.protein |
| Zdroj: | Archives of Microbiology. 182:396-403 |
| ISSN: | 1432-072X 0302-8933 |
| DOI: | 10.1007/s00203-004-0724-y |
| Popis: | D-Amino acid N-acetyltransferase is a unique enzyme of Saccharomyces cerevisiae acting specifically on D-amino acids. The enzyme was found to be encoded by HPA3, a putative histone/protein acetyl transferase gene, and we purified its gene product, Hpa3p, from recombinant Escherichia coli cells. Hpa3p shares 49% sequence identity and 81% sequence similarity with a histone acetyltransferase, Hpa2p, of S. cerevisiae. Hpa3p acts on a wide range of D-amino acids but shows extremely low activity toward histone. However, Hpa2p does not act on any of the free amino acids except L-lysine and D-lysine. Kinetic analyses suggest that Hpa3p catalyzes the N-acetylation of D-amino acids through an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to be liberated. |
| Databáze: | OpenAIRE |
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