EC - L-rhamnose isomerase

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IntEnz Enzyme Nomenclature


Accepted name:
L-rhamnose isomerase
Other names:
L-rhamnose ketol-isomerase
rhamnose isomerase
Systematic name:
L-rhamnose aldose-ketose-isomerase




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 [2].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008740
CAS Registry Number: 9023-84-1
UniProtKB/Swiss-Prot: (72) [show] [UniProt]


  1. Domagk, G.F. and Zech, R.
    Über den Abbau der Desoxyzucker durch Bakterienenzyme. I. L-Rhamnose-Isomerase aus Lactobacillus plantarum.
    Biochem. Z. 339: 145-153 (1963). [PMID: 14095156]
  2. Leang, K., Takada, G., Ishimura, A., Okita, M., Izumori, K.
    Cloning, nucleotide sequence, and overexpression of the L-rhamnose isomerase gene from Pseudomonas stutzeri in Escherichia coli.
    Appl. Environ. Microbiol. 70: 3298-3304 (2004). [PMID: 15184124]
  3. Korndorfer, I. P., Fessner, W. D., Matthews, B. W.
    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.
    J. Mol. Biol. 300: 917-933 (2000). [PMID: 10891278]
  4. Yoshida, H., Yamada, M., Ohyama, Y., Takada, G., Izumori, K., Kamitori, S.
    The structures of L-rhamnose isomerase from Pseudomonas stutzeri in complexes with L-rhamnose and D-allose provide insights into broad substrate specificity.
    J. Mol. Biol. 365: 1505-1516 (2007). [PMID: 17141803]

[EC created 1965]