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Caulobacter crescentus CB15 Reaction: 3.2.1.40

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 3.2.1.40

Enzymes and Genes:
alpha-L-rhamnosidase, putative : CC0978

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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.

Citations: [Rosenfeld65, Kurosawa73, Zverlov00, Yanai00, Cui07, Rabausch14]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:3.2.1.40 , ENZYME:EC:3.2.1.40 , IUBMB-ExplorEnz:EC:3.2.1.40


References

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

Kurosawa73: Kurosawa Y, Ikeda K, Egami F (1973). "-L-rhamnosidases of the liver of Turbo cornutus and Aspergillus niger." J Biochem 73(1);31-7. PMID: 4632197

Rabausch14: Rabausch U, Ilmberger N, Streit WR (2014). "The metagenome-derived enzyme RhaB opens a new subclass of bacterial B type α-L-rhamnosidases." J Biotechnol 191;38-45. PMID: 24815685

Rosenfeld65: Rosenfeld EL, Wiederschein GY (1965). "The metabolism of L-rhamnose in animal tissues." Bull Soc Chim Biol (Paris) 47(7);1433-40. PMID: 5855461

Yanai00: Yanai T, Sato M (2000). "Purification and characterization of an alpha-L-rhamnosidase from Pichia angusta X349." Biosci Biotechnol Biochem 64(10);2179-85. PMID: 11129592

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


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