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Information on EC 3.2.1.40 - alpha-L-rhamnosidase
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3.2.1.40 alpha-L-rhamnosidaseIUBMB 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.
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Word Map
- 3.2.1.40
- l-rhamnose
- decumbens
-
debittering
- hesperidin
- prunin
- grapefruit
- albidus
- food industry
- erubescens
- eupenicillium
-
rhamnosylated
-
hesperidinase
- beta-d-glucosidase
- nutrition
-
alpha-1,2
- gellan
- synthesis
- biotechnology
- industry
- drug development
- degradation
- pharmacology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
naringinase, alpha-l-rhamnosidase, rhab1, rha-p, l-rhamnosidase, rhal1, aorha, pnp-rhamnohydrolase, rhab2, btrha78a, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-L-rhamnosidase
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-
-
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rhamnosidase, alpha -L-
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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PATHWAY SOURCE
PATHWAYS
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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
37288-35-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnose
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-
-
?
hesperidin + H2O
hesperetin 7-glucoside + alpha-L-rhamnose
substrate naringin is preferred over hesperidin
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-
?
naringin + H2O
4',5,7-trihydroxyflavanone-7-beta-D-glucoside + L-rhamnose
substrate naringin is preferred over hesperidin
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-
?
additional information
?
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enzyme is able to hydrolyze alpha-(1-2) amd alpha-(1-6) glycosidic bonds
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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17.9
substrate 4-nitrophenyl alpha-L-rhamnopyranoside, pH 4.0, 40°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
degree of N-glycosylation about 22%, sequence contains 13 putative N-glycosylation sites
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
EXTERNAL LINKS (specific for EC-Number 3.2.1.40)
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Release 2023.1 (January 2023)
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