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Documentos Principais

A1765

Sigma-Aldrich

S-Acetyl-coenzyme A synthetase from baker′s yeast (S. cerevisiae)

lyophilized powder, ≥3 units/mg protein

Sinônimo(s):

Acetate CoA ligase (AMP forming), Acetate thiokinase

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About This Item

Número CAS:
Número da licença da enzima:
Número CE:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.26

Formulário

lyophilized powder

Nível de qualidade

atividade específica

≥3 units/mg protein

composição

Protein, 10-30% biuret

temperatura de armazenamento

−20°C

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Aplicação

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.

Ações bioquímicas/fisiológicas

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 .

Embalagem

Package size based on protein content.

Definição da unidade

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.

forma física

Lyophilized powder containing stabilizers as potassium phosphate, sucrose, and reduced glutathione

Pictogramas

Health hazard

Palavra indicadora

Danger

Frases de perigo

Declarações de precaução

Classificações de perigo

Resp. Sens. 1

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)


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Adenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate are synthesized by yeast acetyl coenzyme A synthetase.
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Journal of Bacteriology, 176(10), 2986-2990 (1994)
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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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