adenylylsulfate-ammonia adenylyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: 5'-adenylyl sulfate + NH4 = adenosine 5'-phosphoramidate + 2 H+ + sulfate. [EC:2.7.7.51, RHEA:19197]

Adenylylsulfate-ammonia adenylyltransferase activity refers to the enzymatic catalysis of the transfer of an adenylyl group from ATP to sulfate, forming adenosine 5'-phosphosulfate (APS). This reaction is a critical step in the assimilation of inorganic sulfate into organic compounds, particularly in the biosynthesis of cysteine and methionine. The enzyme responsible for this activity, adenylylsulfate synthetase (APS synthetase), plays a vital role in sulfur metabolism. The reaction mechanism involves the formation of a transient enzyme-adenylyl-sulfate intermediate, which is then hydrolyzed to release APS and inorganic phosphate. The active site of APS synthetase typically contains a metal ion, such as magnesium or manganese, which is essential for catalytic activity. This enzyme activity is tightly regulated in cells to ensure efficient sulfur assimilation and prevent the accumulation of toxic intermediates. '
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Proteins (1)

Compounds (2)