Coordinated action of pectinesterase and polygalacturonate lyase complex of Clostridium multifermentans.
The polygalacturonate lyase and pectinesterase activities of Clostridium multifermentans, both produced extracellularly when the organism grows on pectin or polygalacturonate, have been suggested to be associated in a single complex. Both enzymic sites act on their respective substrates by single-chain action patterns, as shown by equivalent release of terminal tritium label and total product throughout the reaction. From these results, the Km and V of the lyase, and the amount of lyase activity present, we calculate the steady-state concentration of lyase substrate expected during action of the two sites on pectin if the sites are independent. No such steady-state concentration of lyase substrate was observed. Therefore, we conclude that the two types of active site act in a coordinated manner; the polysaccharide chain passes from the esterase site to the lyase site without intermediate dissociation and rebinding. This 'molecular disassembly line' constituted by the two sites may represent a system of general significance in synthesis and degradation of biological polymers.
D001665:Binding Sites; D002265:Carboxylic Ester Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D003013:Clostridium / Q000201:enzymology*; D007700:Kinetics; D046911:Macromolecular Substances; D009097:Multienzyme Complexes / Q000378:metabolism*; D011133:Polysaccharide-Lyases / Q000302:isolation & purification / Q000378:metabolism*; D011485:Protein Binding
D046911:Macromolecular Substances; D009097:Multienzyme Complexes; D002265:Carboxylic Ester Hydrolases; D011133:Polysaccharide-Lyases