Determinants within the C-terminal domain of Streptomyces lividans acetyl-CoA synthetase that block acetylation of its active site lysine in vitro by the protein acetyltransferase (Pat) enzyme
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Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic StressThe structure of S. lividans acetoacetyl-CoA synthetase shows a novel interaction between the C-terminal extension and the N-terminal domainIn Streptomyces lividans, acetyl-CoA synthetase activity is controlled by O-serine and Nε -lysine acetylation.
P2860
Determinants within the C-terminal domain of Streptomyces lividans acetyl-CoA synthetase that block acetylation of its active site lysine in vitro by the protein acetyltransferase (Pat) enzyme
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name
Determinants within the C-term ...... acetyltransferase (Pat) enzyme
@ast
Determinants within the C-term ...... acetyltransferase (Pat) enzyme
@en
type
label
Determinants within the C-term ...... acetyltransferase (Pat) enzyme
@ast
Determinants within the C-term ...... acetyltransferase (Pat) enzyme
@en
prefLabel
Determinants within the C-term ...... acetyltransferase (Pat) enzyme
@ast
Determinants within the C-term ...... acetyltransferase (Pat) enzyme
@en
P2860
P1433
P1476
Determinants within the C-term ...... acetyltransferase (Pat) enzyme
@en
P2093
Alex C Tucker
Jorge C Escalante-Semerena
P2860
P304
P356
10.1371/JOURNAL.PONE.0099817
P407
P577
2014-06-11T00:00:00Z