EC 3 - Hydrolases
EC 3.2 - Glycosylases
EC 3.2.1 - Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compounds
EC 3.2.1.40 - α-L-rhamnosidase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 3.2.1.40
Names
Accepted name:
α-L-rhamnosidase
Other
names:
α-L-rhamnosidase N
α-L-rhamnosidase T
α-L-rhamnosidase T
Systematic name:
α-L-rhamnoside rhamnohydrolase
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
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
ERGO
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
UniPathway
Gene Ontology:
GO:0030596
CAS Registry Number:
37288-35-0
UniProtKB/Swiss-Prot:
RGXB_ASPNC
References
-
The metabolism of L-rhamnose in animal tissues.Bull. Soc. Chim. Biol. 47: 1433-1440 (1965). [PMID: 5855461]
-
Alpha-L-rhamnosidases of the liver of Turbo cornutus and Aspergillus niger.J. Biochem. 73: 31-37 (1973). [PMID: 4632197]
-
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]
-
Purification and characterization of an alpha-L-rhamnosidase from Pichia angusta X349.Biosci. Biotechnol. Biochem. 64: 2179-2185 (2000). [PMID: 11129592]
-
Crystal structure of glycoside hydrolase family 78 alpha-L-rhamnosidase from Bacillus sp. GL1.J. Mol. Biol. 374: 384-398 (2007). [PMID: 17936784]
-
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]