CATH Classification

Domain Context

CATH Clusters

Superfamily Divalent-metal-dependent TIM barrel enzymes
Functional Family L-rhamnose isomerase

Enzyme Information

5.3.1.14
L-rhamnose isomerase.
based on mapping to UniProt P32170
L-rhamnopyranose = L-rhamnulose.
-!- The enzyme binds the closed ring form of the substrate and catalyzes 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 catalyzes the interconversion of L-mannose and L-fructose, L-lyxose and L-xylulose, D-ribose and D-ribulose, and D-allose and D-psicose.

UniProtKB Entries (1)

P32170
RHAA_ECOLI
Escherichia coli K-12
L-rhamnose isomerase

PDB Structure

PDB 1DE5
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
The structure of rhamnose isomerase from Escherichia coli and its relation with xylose isomerase illustrates a change between inter and intra-subunit complementation during evolution.
Korndorfer, I.P., Fessner, W.D., Matthews, B.W.
J.Mol.Biol.