Michaelis-Menten kinetics can be extended to the case of two turnover sites on a single substrate, even for highly complex non-sequential kinetic schemes. This analysis suggests a general method for extracting enzyme processivity directly from traditional kinetic assays. A preliminary application to experiments involving DNA methylation via DNA adenine methyltransferase (Dam) will be discussed. Similar theoretical considerations, when applied to enzymes with conformational fluctuations, suggest a single criterion sufficient to guarantee Michaelian kinetics. This lone condition subsumes several cases previously described in the literature.