Arsenate closely resembles phosphate, leading to its incorporation into glyceraldehyde-3-phosphate (G3P) by the enzyme GAPDH, which inhibits the enzyme's function. This results in the formation of an unstable arsenate ester that rapidly hydrolyzes in aqueous solutions, preventing the production of the intended product and causing the enzyme to consume G3P without yielding any output. For further details, the study by Crane and Lipmann from 1952 discusses the effects of arsenate on aerobic phosphorylation and provides additional references for deeper insights.