The case study of four FAD-dependent oxidase enzymes is presented in the context of the often-claimed direct electron transfer (DET) to glucose oxidase at carbon nanotubes (CNT). The selected enzymes included d-amino acid (AAOx), alcohol (AOx), pyranose (PyOx), and choline oxidase (ChOx). Each enzyme (E) was mixed with chitosan and CNT (either multi- or single-walled) to form a CNT/E film on the surface of glassy carbon electrode. All eight CNT/E films displayed redox activity depicted by voltammetric current peaks near -0.4 V. However, no DET was observed for any of the films as indicated by the absence of expected substrate- and oxygen-induced asymmetry in the anodic-to-cathodic charge ratio. The peaks are suggested to be due to the redox of either a dissociated FAD cofactor, in the case of AAOx and AOx, or denatured enzyme in the case of PyOx and ChOx. The amperometric assays of the films revealed the lowering of enzymatic activity of all four oxidases by CNT. The results are consistent with the hypothesis of oxidase molecules displaying a spectrum of enzymatic activity in CNT/E films ranging from voltammetrically untraceable (for molecules adsorbed on CNT) to amperometrically measurable (for molecules remote from CNT). The kinetic studies showed that enzyme molecules with no net charge leached at the slowest rate from CNT/E films. This work adds to a growing number of reports challenging the fallacy of DET to FAD-dependent native oxidases.