Representatives of both Streptococcus faecalis and Lactobacillus casei produce isofunctional malic enzymes. All 10 strains of S. faecalis tested could be induced to synthesize malic enzyme and readily adapted to growth on malate. Although 17 of 21 L. casei strains could be induced to produce malic enzyme, only 9 of 14 strains tested grew at the expense of malate. A comparison of catalytic and regulatory properties suggested that the malic enzymes from S. faecalis and L. casei were very similar. Immunological analyses showed that the numerous similarities in function actually reflected partial protein homologies; however, two distinct forms of the malic enzyme were detected among different strains of L. casei by immunochemical and serological procedures. The division of L. casei into two subgroups based on the immunological type of malic enzyme synthesized corresponds to two subspecies currently recognized by microbial taxonomists.An inducible nicotinamide adenine dinucleotide (NAD)-specific malic enzyme from Streptococcus faecalis was shown to be a regulatory protein capable of interacting with three negative effectors which are intermediate products of glucose dissimilation, namely, fructose-1,6-diphosphate (FDP), 3-phosphoglycerate (3PGA), and 6phosphogluconate (6PG; reference 13). A survey of several strains of Lactobacillus casei revealed that at least one of these organisms could also be induced to synthesize an NAD-specific malic enzyme and subsequently grow at the expense of malate. The L. casei malic enzyme bore a striking resemblance to the streptococcal enzyme (London, Meyer, and Kulczyk, Biochim. Biophys. Acta, in press). In addition to similarities in catalytic properties, the Lactobacillus malic enzyme was also inhibited by FDP and 3PGA.A comparison of the physical, catalytic, and regulatory properties of a number of S. faecalis glucose was used to maintain and cultivate the strains of L. casei. Both species were grown as follows. One-126 on July 16, 2020 by guest