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Literature summary for 2.3.1.32 extracted from

  • Mitchell, L.; Lau, A.; Lambert, J.; Zhou, H.; Fong, Y.; Couture, J.; Figeys, D.; Baetz, K.
    Regulation of septin dynamics by the saccharomyces cerevisiae lysine acetyltransferase NuA4 (2011), PLoS ONE, 6, e25336.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
septin protein + acetyl-CoA TAP-tagged septin proteins are cleaved from the magnetic beads during the KAT assay. Multiple sites of acetylation on four of the five yeast mitotic septins, Cdc3, Cdc10, Cdc12 and Shs1 are discovered. In addition to acetylating itself, NuA4 is capable of acetylating Cdc3, Cdc12 and Shs1 in vitro, acetylation on Cdc10 is not detected Saccharomyces cerevisiae ?
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Synonyms

Synonyms Comment Organism
lysine acetyltransferase
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Saccharomyces cerevisiae
NuA4
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Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
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assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
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assay at Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction acetyltransferase-deficient NuA4 mutants have defects in septin collar formation resulting in the development of elongated buds through the Swe1-dependent morphogenesis checkpoint Saccharomyces cerevisiae