ExplorEnz: EC 3.2.1.40

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3.2.1.40

Accepted name:

α-L-rhamnosidase

Reaction:

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

Other name(s):

α-L-rhamnosidase T; α-L-rhamnosidase N

Systematic name:

α-L-rhamnoside rhamnohydrolase

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:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37288-35-0

References:

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

[EC 3.2.1.40 created 1972]