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
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.26
EC Number:
232-729-7
MDL number:
Specific activity:
≥3 units/mg protein
Product Name
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
Storage Class
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
Paul A Lindahl
Journal of inorganic biochemistry, 106(1), 172-178 (2011-11-29)
Nickel-containing carbon monoxide dehydrogenases, acetyl-CoA synthases, nickel-iron hydrogenases, and diron hydrogenases are distinct metalloenzymes yet they share a number of important characteristics. All are O(2)-sensitive, with active-sites composed of iron and/or nickel ions coordinated primarily by sulfur ligands. In each
Jingwen Zhou et al.
Journal of biotechnology, 161(3), 257-264 (2012-07-14)
α-Ketoglutarate (α-KG) is an important intermediate in the tricarboxylic acid (TCA) cycle and has an important role in the regulation of the balance between carbon and nitrogen metabolism in most microorganisms. In previous research, a thiamine-auxotrophic yeast for α-KG overproduction
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
Jessica A M Bastiaansen et al.
Biochimica et biophysica acta, 1830(8), 4171-4178 (2013-04-03)
Acetate metabolism in skeletal muscle is regulated by acetylCoA synthetase (ACS). The main function of ACS is to provide cells with acetylCoA, a key molecule for numerous metabolic pathways including fatty acid and cholesterol synthesis and the Krebs cycle. Hyperpolarized
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