It has been suggested that in spinach leaves an enzyme able to catalyze the phosphorylation of fructose 6‐phosphate to fructose 1,6‐bisphosphate can exist in two different interconvertible forms which use ATP and pyrophosphate respectively as phosphoryl donors [FEBS Letters 169 (1984) 287‐292]. However, the data presented to support this suggestion could also be interpreted without assuming such an unusual type of interconversion. This reinterpretation considers that PFK and PFP are two distinct enzymes which are differentially activated by incubation with various effectors such as UDPG, pyrophosphate, ATP, fructose 6‐phosphate and fructose 2,6‐bisphosphate.