Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.1.40 - alpha-L-rhamnosidase and Organism(s) Bacillus sp. and UniProt Accession Q93RE7

for references in articles please use BRENDA:EC3.2.1.40
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme, found in animal tissues, plants, yeasts, fungi and bacteria, utilizes an inverting mechanism of hydrolysis, releasing beta-L-rhamnose. Substrates include naringin, rutin, quercitrin, hesperidin, dioscin, terpenyl glycosides and many other natural glycosides containing terminal alpha-L-rhamnose.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Bacillus sp.
UNIPROT: Q93RE7
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
naringinase, alpha-l-rhamnosidase, rha-p, rhab1, rhal1, aorha, l-rhamnosidase, btrha78a, btrha, dtrha, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-L-rhamnosidase
-
-
-
-
rhamnosidase, alpha -L-
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-L-rhamnoside rhamnohydrolase
The enzyme, found in animal tissues, plants, yeasts, fungi and bacteria, utilizes an inverting mechanism of hydrolysis, releasing beta-L-rhamnose. Substrates include naringin, rutin, quercitrin, hesperidin, dioscin, terpenyl glycosides and many other natural glycosides containing terminal alpha-L-rhamnose.
CAS REGISTRY NUMBER
COMMENTARY hide
37288-35-0
-