ATP Sulfurylase Yeast

Description

Description:
Recombinant Yeast ATP Sulfurylase is a non-glycosylated, polypeptide chain containing 511 amino acids and having a MW of 57.7 kDa. ATP Sulfurylase catalyzes the activation of sulfate by transferring sulfate to the adenine monophosphate moiety of ATP to form adenosine 5′-phosphosulfate (APS) and pyrophosphate (PPi). The reaction is reversible: ATP is formed from APS and PPi. ATP Sulfurylase is highly purified by proprietary chromatographic techniques.

Source:
Purified from E. coli containing Yeast ATP Sulfurylase gene

Unit Definition:
One unit will produce 1.0 μmole of ATP from APS and inorganic pyrophosphate per min at pH 8.0 at 30°C.

Specific activity:
>2.5u umole/min/mg

Recommended Storage Condition:
-20ºC

Backgroud:
Sulfur metabolism is essential to all organisms. Inorganic sulfate is sequentially activated by ATP Sulfurylase and adenosine 5′-phosphosulfate kinase (APSK). ATP Sulfurylase converts ATP to adenosine-5′-phosphosulfate (APS) and generates pyrophosphate. APSK subsequently phosphorylates APS at the 3’ site to generate 3’‑phosphoadenosine-5′-phosphosulfate (PAPS). PAPS is the sulfur donor required for all sulfotransferase reactions in humans and is also the sulfur source for synthesis of cysteine, methionine and glutathione. The ATP Sulfurylase reaction is highly unfavorable energetically with the standard free-energy change of approximately +46 kJ/mol. To drive the reaction forward, APSK and pyrophosphatase are generally added into the reaction simultaneously to remove the products. The recombinant S. cerevisiae ATP Sulfurylase can be used for in vitro PAPS synthesis.

Additional information

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