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The Drug Target Enzyme Adenosine-5' -Phosphosulfate Reductases in the Sulfate Reductive Pathway from Various Living Organisms

Megan E. Hermann, Myung K. Cho and Sung-Kun Kim

Organisms must metabolize sulfur to survive. The amino acids cysteine and methionine contain sulfur, and essential biomolecules such as thiamine, lipoic acid, and glutathiones also require this element. The most abundant form of sulfur in nature is sulfate. Organisms utilize the sulfate reduction pathway to reduce sulfate to sulfide, which changes the oxidation number from +6 to -2. In order to completely understand the sulfate reductive pathway, gaining knowledge of enzymes that are responsible for the metabolism of sulfur is of paramount importance. There are two branches in the pathway, which require two distinct enzymes: 3’-phosphoadenosine-5’-phosphosulfate (PAPS) reductase and adenosine-5’-phosphosulfate (APS) reductase. While PAPS reductases are found in microbes, APS reductases are found in a variety of organisms, ranging from bacteria to plants. This publication reviews APS reductases in the sulfate reductive pathway from various living organisms and the regulation and inhibition of sulfur metabolism. Since APS reductase is a fundamental enzyme in the element biosynthesis pathway, the enzyme offers an attractive venue for drug discovery.