Description
Contains two divalent metal ions located at different metal-binding sites within the active site. The enzyme binds the closed ring form of the substrate and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. Isomerization proceeds via a hydride-shift mechanism. While the enzyme from the bacterium Escherichia coli is specific for L-rhamnose, the enzyme from the bacterium Pseudomonas stutzeri has broad substrate specificity and catalyses the interconversion of L-mannose and L-fructose, L-lyxose and L-xylulose, D-ribose and D-ribulose, and D-allose and D-psicose