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Key Documents

A1765

Sigma-Aldrich

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:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.26

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

Pictograms

Health hazard

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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
Seunghoon Lee et al.
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
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

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