A1765
S-Acetyl-coenzyme A synthetase from baker′s yeast (S. cerevisiae)
lyophilized powder, ≥3 units/mg protein
Synonyme(s) :
Acetate CoA ligase (AMP forming), Acetate thiokinase
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.26
EC Number:
232-729-7
MDL number:
Specific activity:
≥3 units/mg protein
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Laissez-nous vous aiderNom du produit
S-Acetyl-coenzyme A synthetase from baker′s yeast (S. cerevisiae), lyophilized powder, ≥3 units/mg protein
form
lyophilized powder
specific activity
≥3 units/mg protein
composition
Protein, 10-30% biuret
storage temp.
−20°C
Quality Level
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Application
S-Acetyl-coenzyme A synthetase from baker′s yeast (S. cerevisiae) has been used in the synthesis of adenosine 5′-tetraphosphate and adenosine 5′-pentaphosphate.
S-Acetyl-coenzyme A synthetase may be used to study various metabolic pathways, such as glycolysis, gluconeogenesis, pyruvate metabolism and CO2 fixation. It may also be used in gene expression studies.
Biochem/physiol Actions
Acetyl-coenzyme A synthetase catalyzes the production of acetyl-CoA. It is involved in histone acetylation in the nucleus. It may be involved in the growth of nonfermentable carbon sources such as glycerol. Acetyl-coenzyme A synthetase is induced by acetate, acetaldehyde and ethanol .
Other Notes
One unit will form 1.0 μmole of S-acetyl coenzyme A from acetate, ATP, and coenzyme A per min at pH 7.5 at 37 °C.
Packaging
Package size based on protein content.
Physical form
Lyophilized powder containing stabilizers as potassium phosphate, sucrose, and reduced glutathione
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Classe de stockage
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Heidi A Crosby et al.
The Journal of biological chemistry, 287(19), 15590-15601 (2012-03-15)
N-lysine acetylation is a posttranslational modification that has been well studied in eukaryotes and is likely widespread in prokaryotes as well. The central metabolic enzyme acetyl-CoA synthetase is regulated in both bacteria and eukaryotes by acetylation of a conserved lysine
Hua Xu et al.
Biochemistry, 50(26), 5883-5892 (2011-06-02)
Recent proteomics studies have revealed that protein acetylation is an abundant and evolutionarily conserved post-translational modification from prokaryotes to eukaryotes. Although an astonishing number of acetylated proteins have been identified in those studies, the acetyltransferases that target these proteins remain
Sandy Thao et al.
mBio, 2(5), doi:10-doi:10 (2011-10-20)
In the bacterium Salmonella enterica, the CobB sirtuin protein deacetylase and the Gcn5-related N(ε)-acetyltransferase (GNAT) Pat control carbon utilization and metabolic flux via N(ε)-lysine acetylation/deacetylation of metabolic enzymes. To date, the S. enterica Pat (SePat) acetyltransferase has not been biochemically
Saurabh Sahar et al.
The Journal of biological chemistry, 289(9), 6091-6097 (2014-01-16)
The circadian clock regulates a wide range of physiological and metabolic processes, and its disruption leads to metabolic disorders such as diabetes and obesity. Accumulating evidence reveals that the circadian clock regulates levels of metabolites that, in turn, may regulate
Sara Castaño-Cerezo et al.
Molecular microbiology, 82(5), 1110-1128 (2011-11-09)
Lysine acetylation is a well-established post-translational modification widely conserved and distributed in bacteria. Although multiple regulatory roles have been proved, little is known about its regulation. Here, we present evidence that the transcription of the Gcn5-like acetyltransferase YfiQ of Escherichia
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