EC 3.2.1.40 - α-L-rhamnosidase

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IntEnz Enzyme Nomenclature
EC 3.2.1.40

Names

Accepted name:
α-L-rhamnosidase
Other names:
α-L-rhamnosidase N
α-L-rhamnosidase T
Systematic name:
α-L-rhamnoside rhamnohydrolase

Reaction

Comments:

The enzyme, found in animal tissues, plants, yeasts, fungi and bacteria, utilizes an inverting mechanism of hydrolysis, releasing β-L-rhamnose. Substrates include naringin, rutin, quercitrin, hesperidin, dioscin, terpenyl glycosides and many other natural glycosides containing terminal α-L-rhamnose.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0030596
CAS Registry Number: 37288-35-0
UniProtKB/Swiss-Prot:

References

  1. Rosenfeld, E. and Wiederschein, G.
    The metabolism of L-rhamnose in animal tissues.
    Bull. Soc. Chim. Biol. 47: 1433-1440 (1965). [PMID: 5855461]
  2. Kurosawa, Y., Ikeda, K., Egami, F.
    Alpha-L-rhamnosidases of the liver of Turbo cornutus and Aspergillus niger.
    J. Biochem. 73: 31-37 (1973). [PMID: 4632197]
  3. Zverlov, V. V., Hertel, C., Bronnenmeier, K., Hroch, A., Kellermann, J., Schwarz, W. H.
    The thermostable alpha-L-rhamnosidase RamA of Clostridium stercorarium: biochemical characterization and primary structure of a bacterial alpha-L-rhamnoside hydrolase, a new type of inverting glycoside hydrolase.
    Mol. Microbiol. 35: 173-179 (2000). [PMID: 10632887]
  4. Yanai, T., Sato, M.
    Purification and characterization of an alpha-L-rhamnosidase from Pichia angusta X349.
    Biosci. Biotechnol. Biochem. 64: 2179-2185 (2000). [PMID: 11129592]
  5. Cui, Z., Maruyama, Y., Mikami, B., Hashimoto, W., Murata, K.
    Crystal structure of glycoside hydrolase family 78 alpha-L-rhamnosidase from Bacillus sp. GL1.
    J. Mol. Biol. 374: 384-398 (2007). [PMID: 17936784]
  6. Rabausch, U., Ilmberger, N., Streit, W. R.
    The metagenome-derived enzyme RhaB opens a new subclass of bacterial B type alpha-L-rhamnosidases.
    J. Biotechnol. 191: 38-45 (2014). [PMID: 24815685]

[EC 3.2.1.40 created 1972]