IntEnz

EC 3.2.1.40 - α-L-rhamnosidase

IntEnz Enzyme Nomenclature
EC 3.2.1.40

Names

Reaction

• Hydrolysis of terminal non-reducing α-L-rhamnose residues in α-L-rhamnosides

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

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]