Coimmobilized multienzymes: an in vitro model for cellular processes.
Two different systems of multienzymes have been coimmobilized onto Sepharose and shown to be catalytically active. The first system consists of the five enzymes that catalyze the conversion of glucose 1-phosphate to 1,3-diphosphoglycerate along with the bacterial enzymes which are used to monitor NADH production by light emission. The NADH:FMN oxidoreductase-luciferase enzymes act to "pull" the reactions by continually oxidizing the NADH formed. The second system consisted of the 11 enzymes necessary for the conversion of glucose to alcohol and the bacterial enzymes. In the presence of excess glucose this immobilized system was able to produce 4068 nmol of alcohol per gram of Sepharose-enzymes in 4 h. Using the same system, if 3-phosphoglycerate was used as the substrate, 6552 nmol of alcohol were formed. These multienzyme immobilized systems are models that are uniquely suited for comparative studies of metabolic processes that occur in intact cells.
D000818:Animals; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005958:Glucosephosphates / Q000378:metabolism; D007700:Kinetics; D008954:Models, Biological; D009097:Multienzyme Complexes / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D010084:Oxidation-Reduction; D012685:Sepharose
D004800:Enzymes, Immobilized; D005958:Glucosephosphates; D009097:Multienzyme Complexes; D009243:NAD; D012685:Sepharose; C031590:glucose-1-phosphate