A1765
S-Acetyl-coenzyme A synthetase from baker′s yeast (S. cerevisiae)
lyophilized powder, ≥3 units/mg protein
Synonym(s):
Acetate CoA ligase (AMP forming), Acetate thiokinase
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About This Item
Recommended Products
form
lyophilized powder
Quality Level
specific activity
≥3 units/mg protein
composition
Protein, 10-30% biuret
storage temp.
−20°C
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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 .
Packaging
Package size based on protein content.
Unit Definition
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.
Physical form
Lyophilized powder containing stabilizers as potassium phosphate, sucrose, and reduced glutathione
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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
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
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
Eukaryotic cell, 10(8), 1043-1052 (2011-06-15)
Acetyl coenzyme A (acetyl-CoA) is a crucial metabolite for energy metabolism and biosynthetic pathways and is produced in various cellular compartments with spatial and temporal precision. Our previous study on ATP citrate lyase (ACL) in Gibberella zeae revealed that ACL-dependent
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
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