|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 220.127.116.11
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
Mass balance status: Marked as unbalanced.
Enzyme Commission Primary Name: α-L-rhamnosidase
Enzyme Commission Synonyms: α-L-rhamnosidase T, α-L-rhamnosidase N
Enzyme Commission Summary:
This enzyme catalyzes the hydrolysis of terminal non-reducing α-L-rhamnose residues in α-L-rhamnosides. The enzyme, found in animal tissues, plants, yeasts, fungi and bacteria, utilizes an inverting mechanism of hydrolysis, releasing β-L-rhamnopyranose. Substrates include naringin, rutin, quercitrin, hesperidin, dioscin, terpenyl glycosides and many other natural glycosides containing terminal α-L-rhamnose.
Cui07: Cui Z, Maruyama Y, Mikami B, Hashimoto W, Murata K (2007). "Crystal structure of glycoside hydrolase family 78 alpha-L-Rhamnosidase from Bacillus sp. GL1." J Mol Biol 374(2);384-98. PMID: 17936784
Zverlov00: Zverlov VV, Hertel C, Bronnenmeier K, Hroch A, Kellermann J, Schwarz WH (2000). "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(1);173-9. PMID: 10632887
©2016 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493