Glycolytic enzymes are responsible for conversion of glucose to pyruvate. It is well known that glycolytic enzymes can form dynamic complexes and substrate channeling in such complexes may take place. A number of in vitro methods have been used to investigate interaction between enolase and phosphoglycerate mutase. To determine whether this interaction is "visible" with the help of computer modeling method, two different enolases have been chosen from available protein data banks. Saccharomyces Cerevisiae (Sc.) phosphoglycerate mutase and Sc. enolase dimers together with Trypanosoma brucei (TB) enolase monomer have been tested for interaction. Analysis showed that 70% of most active binding amino acid residues of TB enolase are identical to residues of yeast enolase. Nevertheless no channeling has been observed.