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Information on EC 3.2.1.40 - alpha-L-rhamnosidase
for references in articles please use BRENDA:EC3.2.1.40
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EC Tree 3 Hydrolases
3.2 Glycosylases
3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
3.2.1.40 alpha-L-rhamnosidase
IUBMB 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.
The enzyme appears in viruses and cellular organisms
- 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
Reaction Schemes
showSynonyms
naringinase, alpha-l-rhamnosidase, rhab1, rha-p, aorha, l-rhamnosidase, rhal1, dtrha, pnp-rhamnohydrolase, rhab2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-L-rhamnosidase
alpha-RHA
AnigIFM63604_006389
AoRha
Athe_2581
AtRha
BtRha
BtRha78A
Cb_Ram106B
Cst_c00400
CTN_1495
dicth_0289
DthRha
DtRha
EC 3.2.1.66
-
-
formerly
-
GH78 alpha-L-rhamnosidase
KoRha
lp_3471
lp_3473
N12-Rha
naringinase
PodoRha
r-Rha1
ram
Ram1
Ram2
RamALA
RHA
Rha-N1
RHA-P
RhaA
RhaB
RhaB1
RhaB2
RhaL1
Rham
rhamnosidase, alpha -L-
-
-
-
-
Rhase-TS
SAVERM_828
Tmari_1078
Tm_Ram106B
Tn_Ram106B
TpeRha
tpet_1682
TstRhaA
Ts_Ram106B
additional information
alpha-L-rhamnosidase
-
-
-
-
additional information
-
narginase: complex of beta-D-glucosidase and alpha-L-rhamnosidase
additional information
-
narginase: complex of beta-D-glucosidase and alpha-L-rhamnosidase
additional information
-
narginase: complex of beta-D-glucosidase and alpha-L-rhamnosidase
additional information
the enzyme belongs to the bacterial subfamily of the glycoside hydrolase family 2
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of terminal non-reducing alpha-L-rhamnose residues in alpha-L-rhamnosides
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
rutin degradation (plants)
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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.
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CAS REGISTRY NUMBER
COMMENTARY
37288-35-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-deoxy-5-fluorouridine + L-rhamnose
?
Substrates: rhamnosylation reaction
Products: -
Products: -
?
2-phenylethyl beta-D-rutinoside + H2O
2-phenylethyl beta-D-glucopyranoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
20(S)-ginsenoside Rg2 + H2O
20(S)-ginsenoside Rh1 + alpha-L-rhamnose
-
Substrates: low activity cleaving the alpha-1,2-linkage
Products: -
Products: -
?
3-O-alpha-L-rhamnopyranosyl-alpha-D-mannopyranoside + H2O
alpha-L-rhamnose + alpha-D-mannose
-
Substrates: -
Products: -
Products: -
?
4',5,7-trihydroxyflavanone 7-rhamnoglucoside + H2O
4',5,7-trihydroxyflavanone 7-glucoside + alpha-L-rhamnose
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
Substrates: -
Products: 2.1% of activity compared to p-nitrophenyl-alpha-L-rhamnopyranoside
Products: 2.1% of activity compared to p-nitrophenyl-alpha-L-rhamnopyranoside
?
4-nitrophenyl-alpha-L-rhamnopyranoside + H2O
alpha-L-rhamnose + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
6-O-alpha-L-rhamnosyl-D-glucopyranose + H2O
alpha-L-rhamnose + D-glucose
-
Substrates: rutinose
Products: -
Products: -
?
convallotoxin + H2O
strophantidin + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
cytosine arabinoside + L-rhamnose
?
Substrates: rhamnosylation reaction
Products: -
Products: -
?
dulcoside A + H2O
rubusoside + alpha-L-rhamnose
Substrates: no hydrolytic activity against dulcoside A analogues. No transrhamnosylation activity is observed
Products: -
Products: -
?
frangulin + H2O
frangula emodin + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
geranyl-beta-D-rutinoside + H2O
geranyl-beta-D-glycoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
ginsenoside Rg2 + H2O
ginsenoside Rh1 + alpha-L-rhamnose
Substrates: low activity
Products: -
Products: -
?
hesperidin + H2O
? + alpha-L-rhamnose
Substrates: cleavage of the alpha-1,6-linkage
Products: -
Products: -
?
hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + L-rhamnose
-
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
L-rhamnose + ?
Substrates: -
Products: -
Products: -
?
high-methoxyl pectin + H2O
pyranoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
hydroxyurea + L-rhamnose
?
Substrates: rhamnosylation reaction
Products: -
Products: -
?
methyl 3-O-alpha-L-rhamnopyranosyl-alpha-D-mannopyranoside + H2O
alpha-L-rhamnose + methyl alpha-D-mannose
-
Substrates: -
Products: -
Products: -
?
methyl 3-O-alpha-L-rhamnopyranosyl-alpha-D-xylopyranoside + H2O
alpha-L-rhamnose + methyl alpha-D-xylose
-
Substrates: -
Products: -
Products: -
?
methyl 3-O-alpha-L-rhamnopyranosyl-alpha-L-rhamnopyranoside + H2O
alpha-L-rhamnose + methyl alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
methyl 4-O-alpha-L-rhamnopyranosyl-alpha-D-galactopyranoside + H2O
alpha-L-rhamnose + methyl alpha-D-galactose
-
Substrates: -
Products: -
Products: -
?
methyl 4-O-alpha-L-rhamnopyranosyl-alpha-D-mannopyranoside + H2O
alpha-L-rhamnose + methyl alpha-D-mannose
-
Substrates: -
Products: -
Products: -
?
methyl 4-O-alpha-L-rhamnopyranosyl-alpha-D-xylopyranoside + H2O
alpha-L-rhamnose + alpha-D-xylose
-
Substrates: -
Products: -
Products: -
?
muscat glycoside extract
linalool + alpha-terpineol + citronellol + nerol + geraniol + ?
-
Substrates: -
Products: -
Products: -
?
myricetrin + H2O
3,5,7-trihydroxy-2-(3,4,5-trihydroxyphenyl)-4H-chromen-4-one + alpha-L-rhamnose
myricitrin + H2O
3,5,7-trihydroxy-2-(3,4,5-trihydroxyphenyl)-4H-chromen-4-one + alpha-L-rhamnose
myricitrin + H2O
L-rhamnose + myricetin
-
Substrates: myricitrin is identical with myricetin-3-L-rhamnoside
Products: -
Products: -
?
naringin + H2O
4',5,7-trihydroxyflavanone 7-O-beta-D-glucoside + L-rhamnose
-
Substrates: -
Products: -
Products: -
?
naringin + H2O
4',5,7-trihydroxyflavanone-7-beta-D-glucoside + L-rhamnose
Substrates: substrate naringin is preferred over hesperidin
Products: -
Products: -
?
naringin + H2O
? + alpha-L-rhamnose
Substrates: preferred substrate, cleavage of the alpha-1,2-linkage
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
narirutin + H2O
? + L-rhamnose
-
Substrates: isonaringin, high activity
Products: -
Products: -
?
neohesperidin + H2O
5-hydroxy-2-(3-hydroxy-4-methoxyphenyl)-4-oxo-3,4-dihydro-2H-chromen-7-yl beta-D-glucopyranoside + alpha-L-rhamnose
neohesperidin dihydrochalcone + H2O
3,5-dihydroxy-4-[3-(3-hydroxy-4-methoxyphenyl)propanoyl]phenyl beta-D-glucopyranoside + alpha-L-rhamnose
F6IEX3
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-arabinofuranoside + H2O
p-nitrophenol + alpha-L-arabinofuranose
-
Substrates: -
Products: 6.1% of activity compared to p-nitrophenyl-alpha-L-rhamnopyranoside
Products: 6.1% of activity compared to p-nitrophenyl-alpha-L-rhamnopyranoside
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
p-nitrophenol + beta-D-galactopyranose
Q93RE8, Q93RE7
Substrates: -
Products: 1.6% of activity compared to p-nitrophenyl-alpha-L-rhamnopyranoside
Products: 1.6% of activity compared to p-nitrophenyl-alpha-L-rhamnopyranoside
?
periplor alpha-L-rhamnoside + H2O
periplogenin + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
polygalacturonic acid + H2O
D-galacturonic acid
-
Substrates: -
Products: -
Products: -
?
proscillaridin A + H2O
pyranosyl 3,14-dihydroxybufa-4,20,22-trienolid + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
quercetin 3-alpha-L-rhamnopyranoside + H2O
quercetin + L-rhamnose
-
Substrates: 31% of activity compared to naringin
Products: -
Products: -
?
rhamnogalacturonan tetramer + H2O
?
Substrates: -
Products: -
Products: -
?
robinin + H2O
rhamnose + kaempferol-3-robinoside
-
Substrates: robinin is identical with kaempferol-3-robinoside-7-rhamnoside
Products: -
Products: -
?
rutin + H2O
? + alpha-L-rhamnose
Substrates: low activity, cleavage of the alpha-1,6-linkage
Products: -
Products: -
?
saikosaponin C + H2O
(3beta,16beta)-16-hydroxy-13,28-epoxyolean-11-en-3-yl) 6-O-beta-D-glucopyranosyl-beta-D-glucopyranoside + alpha-L-rhamnose
scilliglaucosidin alpha-L-rhamnoside + H2O
scilliglaucosidin + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
scilliphaeosidin alpha-L-rhamnoside + H2O
scilliphaeosidin + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
4',5,7-trihydroxyflavanone 7-rhamnoglucoside + H2O
4',5,7-trihydroxyflavanone 7-glucoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
4',5,7-trihydroxyflavanone 7-rhamnoglucoside + H2O
4',5,7-trihydroxyflavanone 7-glucoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
4',5,7-trihydroxyflavanone 7-rhamnoglucoside + H2O
4',5,7-trihydroxyflavanone 7-glucoside + alpha-L-rhamnose
-
Substrates: rhamnosidase N, naringin
Products: -
Products: -
?
4',5,7-trihydroxyflavanone 7-rhamnoglucoside + H2O
4',5,7-trihydroxyflavanone 7-glucoside + alpha-L-rhamnose
Bacteroides JY-6
-
Substrates: -
Products: -
Products: -
?
4',5,7-trihydroxyflavanone 7-rhamnoglucoside + H2O
4',5,7-trihydroxyflavanone 7-glucoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
4',5,7-trihydroxyflavanone 7-rhamnoglucoside + H2O
4',5,7-trihydroxyflavanone 7-glucoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
4',5,7-trihydroxyflavanone 7-rhamnoglucoside + H2O
4',5,7-trihydroxyflavanone 7-glucoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
4',5,7-trihydroxyflavanone 7-rhamnoglucoside + H2O
4',5,7-trihydroxyflavanone 7-glucoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Alternaria alternata SK37.001
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Substrates: 70.1% of the activity compared to naringin
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Aspergillus niger JMU-TS528
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Aspergillus niger JMU-TS528
Substrates: 70.1% of the activity compared to naringin
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Aspergillus oryzae NL-1
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Substrates: no activity with 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-xyloside, 4-nitrophenyl beta-D-arabinofuranoside, 4-nitrophenyl beta-D-arabinopyranoside, 4-nitrophenyl beta-D-galactopyranoside
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Substrates: no activity with 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-xyloside, 4-nitrophenyl beta-D-arabinofuranoside, 4-nitrophenyl beta-D-arabinopyranoside, 4-nitrophenyl beta-D-galactopyranoside
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Fusarium verticillioides MTCC-2088
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
F6IEX3
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Aspergillus niger ATCC MYA-4892
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Aspergillus niger CCTCC M 2018240
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Aspergillus niger FGSC A1513
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Aspergillus terreus CCF3059
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Lactiplantibacillus plantarum ATCC BAA-793
Substrates: -
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Lactiplantibacillus plantarum NCIMB 8826
Substrates: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
-
Substrates: -
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
-
Substrates: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
-
Substrates: 91% conversion
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
R4P072
Substrates: -
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
R4P072
Substrates: -
Products: -
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
R4P072
Substrates: -
Products: -
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
R4P072
Substrates: -
Products: -
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
R4P072
Substrates: -
Products: -
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl alpha-L-rhamnoside + H2O
alpha-L-rhamnose + 4-nitrophenol
-
Substrates: -
Products: -
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4-nitrophenyl alpha-L-rhamnoside + H2O
alpha-L-rhamnose + 4-nitrophenol
Substrates: -
Products: -
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4-nitrophenyl alpha-L-rhamnoside + H2O
alpha-L-rhamnose + 4-nitrophenol
Substrates: -
Products: -
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4-nitrophenyl alpha-L-rhamnoside + H2O
alpha-L-rhamnose + 4-nitrophenol
-
Substrates: -
Products: -
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4-nitrophenyl-alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Q93RE7
Substrates: -
Products: -
Products: -
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4-nitrophenyl-alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
Q93RE7
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
-
Substrates: -
Products: -
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4-nitrophenyl-alpha-L-rhamnopyranoside + H2O
4-nitrophenol + L-rhamnopyranose
-
Substrates: -
Products: -
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?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
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alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
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alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
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alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
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alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
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alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
Bacteroides JY-6
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
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alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
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alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
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alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
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alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
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alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
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alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
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baohuoside I + H2O
icaritin + L-rhamnose
Substrates: -
Products: -
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epimedin C + H2O
icariin + alpha-L-rhamnopyranose
Substrates: -
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epimedin C + H2O
icariin + alpha-L-rhamnopyranose
Substrates: -
Products: -
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epimedin C + H2O
icariin + L-rhamnose
-
Substrates: -
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epimedin C + H2O
icariin + L-rhamnose
-
Substrates: -
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epimedin C + H2O
icariin + L-rhamnose
-
Substrates: the icariin yield increases from 61% to over 83% after optimization of the reaction method, detailed overview. The bioconversion of epimedin C into icariin can reach 90.5% under the optimum conditions
Products: -
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epoetin C + H2O
icariin + L-rhamnose
-
Substrates: -
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epoetin C + H2O
icariin + L-rhamnose
-
Substrates: -
Products: -
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gellan + H2O
alpha-L-rhamnose + ?
Q93RE7
Substrates: hydrolytic reaction, release of rhamnose from the disaccharide
Products: -
Products: -
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gellan + H2O
alpha-L-rhamnose + ?
Q93RE7
Substrates: release of rhamnose from the substrate, hydrolytic reaction
Products: -
Products: -
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gellan + H2O
alpha-L-rhamnose + ?
Q93RE7
Substrates: release of rhamnose from the disaccharide, hydrolytic reaction
Products: residues interacting with rhamnose that are crucial for enzyme catalysis and/or substrate binding identified by crystallization
Products: residues interacting with rhamnose that are crucial for enzyme catalysis and/or substrate binding identified by crystallization
?
gellan + H2O
alpha-L-rhamnose + ?
Q93RE7
Substrates: hydrolytic reaction, release of rhamnose from the disaccharide
Products: -
Products: -
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gellan + H2O
alpha-L-rhamnose + ?
Q93RE7
Substrates: release of rhamnose from the substrate, hydrolytic reaction
Products: -
Products: -
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gellan + H2O
alpha-L-rhamnose + ?
Q93RE7
Substrates: release of rhamnose from the disaccharide, hydrolytic reaction
Products: residues interacting with rhamnose that are crucial for enzyme catalysis and/or substrate binding identified by crystallization
Products: residues interacting with rhamnose that are crucial for enzyme catalysis and/or substrate binding identified by crystallization
?
gellan + H2O
L-rhamnose + ?
Q93RE8, Q93RE7
Substrates: -
Products: -
Products: -
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gellan + H2O
L-rhamnose + ?
Q93RE8, Q93RE7
Substrates: -
Products: -
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gypenoside-5 + H2O
ginsenoside Rd + alpha-L-rhamnose
-
Substrates: -
Products: -
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gypenoside-5 + H2O
ginsenoside Rd + alpha-L-rhamnose
-
Substrates: cleavage of the alpha-1,6-linkage
Products: -
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hesperidin + H2O
?
-
Substrates: 34% of activity compared to naringin
Products: -
Products: -
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hesperidin + H2O
?
-
Substrates: 97% conversion, hydrolysis of alpha-1,2-linked rhamnose
Products: -
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hesperidin + H2O
hesperetin 7-glucoside + alpha-L-rhamnose
-
Substrates: -
Products: -
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hesperidin + H2O
hesperetin 7-glucoside + alpha-L-rhamnose
Substrates: substrate naringin is preferred over hesperidin
Products: -
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hesperidin + H2O
hesperetin 7-glucoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin 7-glucoside + alpha-L-rhamnose
Bacteroides JY-6
-
Substrates: -
Products: -
Products: -
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hesperidin + H2O
hesperetin 7-glucoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin 7-glucoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin 7-glucoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
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hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
Alternaria alternata SK37.001
-
Substrates: -
Products: -
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hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
Substrates: -
Products: -
Products: -
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hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
Substrates: 144.9% of the activity compared to naringin
Products: -
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hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
Aspergillus niger JMU-TS528
Substrates: -
Products: -
Products: -
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hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
Aspergillus niger JMU-TS528
Substrates: 144.9% of the activity compared to naringin
Products: -
Products: -
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hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
-
Substrates: 134% of the activity compared to 4-nitrophenyl-alpha-L-rhamnopyranoside
Products: -
Products: -
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hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
-
Substrates: 240.6% of the activity with rutin
Products: -
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hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
Aspergillus oryzae NL-1
-
Substrates: 240.6% of the activity with rutin
Products: -
Products: -
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hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
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hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
Fusarium verticillioides MTCC-2088
-
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
F6IEX3
Substrates: -
Products: -
Products: -
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hesperidin + H2O
hesperetin 7-O-glucoside + alpha-L-rhamnose
Substrates: isoform RhaB2 exhibits highest activity against hesperidin
Products: -
Products: -
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hesperidin + H2O
hesperetin 7-O-glucoside + alpha-L-rhamnose
Substrates: 11.2% relative activity compared to rutin
Products: -
Products: -
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hesperidin + H2O
hesperetin 7-O-glucoside + alpha-L-rhamnose
Substrates: isoform RhaB2 exhibits highest activity against hesperidin
Products: -
Products: -
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hesperidin + H2O
hesperetin 7-O-glucoside + alpha-L-rhamnose
Substrates: 11.2% relative activity compared to rutin
Products: -
Products: -
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hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
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hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Aspergillus niger ATCC MYA-4892
Substrates: -
Products: -
Products: -
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hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
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hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Aspergillus niger CCTCC M 2018240
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Aspergillus niger CCTCC M 2018240
Substrates: -
Products: -
Products: -
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hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Aspergillus niger FGSC A1513
Substrates: -
Products: -
Products: -
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hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Aspergillus niger JMU-TS528
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: best substrate
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Q93RE8, Q93RE7
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Bacteroides thetaiotaomicron CCUG 10774
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Bacteroides thetaiotaomicron JCM 5827
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Klebsiella oxytoca BUCSAV 143
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Klebsiella oxytoca CCM 1901
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Lactiplantibacillus plantarum ATCC BAA-793
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Lactiplantibacillus plantarum NCIMB 8826
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
F6IEX3
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: low activity
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Papiliotrema laurentii ZJU-L07
-
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Talaromyces stollii CLY-6
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: 87.6% activity compared to rutin
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: 87.6% activity compared to rutin
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
icariin + H2O
icarisid I + L-rhamnose
Substrates: enzyme AtRha can hydrolyze icariin containing the alpha-1 rhamnoside linkage
Products: -
Products: -
?
icariin + H2O
icarisid I + L-rhamnose
Aspergillus terreus CCF3059
Substrates: enzyme AtRha can hydrolyze icariin containing the alpha-1 rhamnoside linkage
Products: -
Products: -
?
myricetrin + H2O
3,5,7-trihydroxy-2-(3,4,5-trihydroxyphenyl)-4H-chromen-4-one + alpha-L-rhamnose
Substrates: 22.5% of the activity compared to naringin
Products: -
Products: -
?
myricetrin + H2O
3,5,7-trihydroxy-2-(3,4,5-trihydroxyphenyl)-4H-chromen-4-one + alpha-L-rhamnose
Aspergillus niger JMU-TS528
Substrates: 22.5% of the activity compared to naringin
Products: -
Products: -
?
myricitrin + H2O
3,5,7-trihydroxy-2-(3,4,5-trihydroxyphenyl)-4H-chromen-4-one + alpha-L-rhamnose
Substrates: low activity
Products: -
Products: -
?
myricitrin + H2O
3,5,7-trihydroxy-2-(3,4,5-trihydroxyphenyl)-4H-chromen-4-one + alpha-L-rhamnose
Aspergillus niger JMU-TS528
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
4',5,7-trihydroxyflavanone-7-beta-D-glucoside + alpha-L-rhamnose
Q93RE7
Substrates: bitter flavour source in fruit
Products: -
Products: -
?
naringin + H2O
4',5,7-trihydroxyflavanone-7-beta-D-glucoside + alpha-L-rhamnose
Q93RE7
Substrates: bitter flavour source in fruit
Products: -
Products: -
?
naringin + H2O
4',5,7-trihydroxyflavanone-7-beta-D-glucoside + alpha-L-rhamnose
Substrates: bitter flavour source in fruit, design of a bioreactor producing alpha-L-rhamnose
Products: -
Products: -
?
naringin + H2O
?
-
Substrates: 98% conversion, hydrolysis of alpha-1,2-linked rhamnose
Products: -
Products: -
?
naringin + H2O
?
Substrates: citrus peel naringin
Products: -
Products: -
?
naringin + H2O
?
Substrates: the free and immobilized enzymes achieve 76% and 67% hydrolysis of the naringin in Kinnow juice, respectively
Products: -
Products: -
?
naringin + H2O
? + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
Alternaria alternata SK37.001
-
Substrates: -
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
Aspergillus niger JMU-TS528
Substrates: -
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
-
Substrates: 26% of the activity compared to 4-nitrophenyl-alpha-L-rhamnopyranoside
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
-
Substrates: 21% of the activity with rutin
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
Aspergillus oryzae NL-1
-
Substrates: 21% of the activity with rutin
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
Substrates: the enzyme shows a strong ability to hydrolyze naringin but scarcely acts on other substrates. It shows negligible activities on rutin, hesperidin, quercitrin, ginsenoside Rg2, myricitrin, saikosaponin C and 4-nitrophenyl-alpha-L-rhamnoside
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
Aspergillus tubingensis JMU-TS529
Substrates: the enzyme shows a strong ability to hydrolyze naringin but scarcely acts on other substrates. It shows negligible activities on rutin, hesperidin, quercitrin, ginsenoside Rg2, myricitrin, saikosaponin C and 4-nitrophenyl-alpha-L-rhamnoside
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
Bacteroides JY-6
-
Substrates: -
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
Fusarium verticillioides MTCC-2088
-
Substrates: -
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
F6IEX3
Substrates: -
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
naringin + H2O
L-rhamnose + ?
Substrates: -
Products: -
Products: -
?
naringin + H2O
L-rhamnose + ?
Q93RE8, Q93RE7
Substrates: -
Products: -
Products: -
?
naringin + H2O
L-rhamnose + ?
Q93RE8, Q93RE7
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Aspergillus niger CCTCC M 2018240
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Aspergillus niger JMU-TS528
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Q93RE8, Q93RE7
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Bacteroides thetaiotaomicron CCUG 10774
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Bacteroides thetaiotaomicron JCM 5827
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Klebsiella oxytoca BUCSAV 143
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Klebsiella oxytoca CCM 1901
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Lactiplantibacillus plantarum ATCC BAA-793
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Lactiplantibacillus plantarum NCIMB 8826
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
F6IEX3
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: high activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Talaromyces stollii CLY-6
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: 31.0% activity compared to rutin
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: 31.0% activity compared to rutin
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
R4P072
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
R4P072
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
R4P072
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
R4P072
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
R4P072
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: low activity
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin dihydrochalcone + H2O
trilobatin + alpha-L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin dihydrochalcone + H2O
trilobatin + alpha-L-rhamnose
Aspergillus niger JMU-TS528
Substrates: -
Products: -
Products: -
?
narirutin + H2O
?
-
Substrates: 60% conversion, hydrolysis of alpha-1,6-linked rhamnose
Products: -
Products: -
?
neohesperidin + H2O
5-hydroxy-2-(3-hydroxy-4-methoxyphenyl)-4-oxo-3,4-dihydro-2H-chromen-7-yl beta-D-glucopyranoside + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
neohesperidin + H2O
5-hydroxy-2-(3-hydroxy-4-methoxyphenyl)-4-oxo-3,4-dihydro-2H-chromen-7-yl beta-D-glucopyranoside + alpha-L-rhamnose
Bacteroides JY-6
-
Substrates: -
Products: -
Products: -
?
neohesperidin + H2O
?
-
Substrates: 70% conversion, hydrolysis of alpha-1,6-linked rhamnose
Products: -
Products: -
?
neohesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: low activity
Products: -
Products: -
?
neohesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: -
Products: -
Products: -
?
neohesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: high activity
Products: -
Products: -
?
neohesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Papiliotrema laurentii ZJU-L07
-
Substrates: -
Products: -
Products: -
?
notoginsenoside R1 + H2O
?
-
Substrates: -
Products: -
Products: -
?
p-nitrophenol-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: assay reaction system to determine enzyme activity in psychrophile bacteria, at 25°C and at 5°C
Products: -
Products: -
?
p-nitrophenol-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: assay reaction system to determine enzyme activity in psychrophile bacteria
Products: -
Products: -
?
p-nitrophenyl alpha-L-rhamnoside + H2O
p-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-rhamnoside + H2O
p-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-rhamnoside + H2O
p-nitrophenol + alpha-L-rhamnose
-
Substrates: single displacement reaction mechanism
Products: -
Products: -
?
p-nitrophenyl alpha-L-rhamnoside + H2O
p-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-rhamnoside + H2O
p-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-rhamnoside + H2O
p-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-rhamnoside + H2O
p-nitrophenol + alpha-L-rhamnose
Bacteroides JY-6
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-rhamnoside + H2O
p-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-rhamnoside + H2O
p-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-rhamnoside + H2O
p-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-rhamnoside + H2O
p-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-rhamnoside + H2O
p-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-rhamnoside + H2O
p-nitrophenol + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
Q93RE8, Q93RE7
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
Q93RE7
Substrates: assay reaction system to determine activity of wild-type and mutant enzymes
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
Q93RE8, Q93RE7
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
Q93RE7
Substrates: assay reaction system to determine activity of wild-type and mutant enzymes
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
Bacteroides JY-6
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
Substrates: assay reaction system to determine enzyme activity in small and large experiments for bioreactor efficiency
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-fucopyranoside + H2O
p-nitrophenol + beta-D-fucopyranose
Q93RE8, Q93RE7
Substrates: -
Products: 2.9% of activity compared to p-nitrophenyl-alpha-L-rhamnopyranoside
Products: 2.9% of activity compared to p-nitrophenyl-alpha-L-rhamnopyranoside
?
p-nitrophenyl-beta-D-fucopyranoside + H2O
p-nitrophenol + beta-D-fucopyranose
Q93RE8, Q93RE7
Substrates: -
Products: 2.9% of activity compared to p-nitrophenyl-alpha-L-rhamnopyranoside
Products: 2.9% of activity compared to p-nitrophenyl-alpha-L-rhamnopyranoside
?
proscillaridin A + H2O
?
Substrates: 0.4% relative activity compared to hesperidin
Products: -
Products: -
?
proscillaridin A + H2O
?
Substrates: 4.5% relative activity compared to rutin
Products: -
Products: -
?
quercitrin + H2O
quercetin + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
quercitrin + H2O
quercetin + alpha-L-rhamnose
Alternaria alternata SK37.001
-
Substrates: -
Products: -
Products: -
?
quercitrin + H2O
quercetin + alpha-L-rhamnose
F6IEX3
Substrates: -
Products: -
Products: -
?
quercitrin + H2O
quercetin + L-rhamnose
-
Substrates: -
Products: -
Products: -
?
quercitrin + H2O
quercetin + L-rhamnose
-
Substrates: quercitrin is identical with quercetin-3-L-rhamnoside
Products: -
Products: -
?
quercitrin + H2O
quercetin + L-rhamnose
-
Substrates: quercitrin is identical with quercetin 3-L-rhamnoside, growth on quercitrin as carbon source
Products: -
Products: -
?
quercitrin + H2O
quercetin + L-rhamnose
-
Substrates: -
Products: -
Products: -
?
quercitrin + H2O
quercetin + L-rhamnose
-
Substrates: -
Products: -
Products: -
?
quercitrin + H2O
quercetin + L-rhamnose
-
Substrates: rhamnosidase T
Products: -
Products: -
?
rhamnosyl-glucose + H2O
glucose + alpha-L-rhamnose
-
Substrates: gellan as carbon-source
Products: -
Products: -
?
rhamnosyl-glucose + H2O
glucose + alpha-L-rhamnose
-
Substrates: gellan as carbon-source
Products: -
Products: -
?
rutin + H2O
3-glycosylquercetin + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
rutin + H2O
3-glycosylquercetin + alpha-L-rhamnose
-
Substrates: rhamnosidase N
Products: -
Products: -
?
rutin + H2O
3-glycosylquercetin + alpha-L-rhamnose
Bacteroides JY-6
-
Substrates: -
Products: -
Products: -
?
rutin + H2O
3-glycosylquercetin + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
rutin + H2O
3-glycosylquercetin + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
rutin + H2O
?
-
Substrates: 63% of activity compared to naringin
Products: -
Products: -
?
rutin + H2O
?
-
Substrates: 10% conversion, hydrolysis of alpha-1,6-linked rhamnose
Products: -
Products: -
?
rutin + H2O
? + L-rhamnose
Substrates: best substrate
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Aspergillus niger CCTCC M 2018240
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Aspergillus niger JMU-TS528
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Q93RE8, Q93RE7
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Bacteroides thetaiotaomicron CCUG 10774
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Bacteroides thetaiotaomicron JCM 5827
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Klebsiella oxytoca BUCSAV 143
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Klebsiella oxytoca CCM 1901
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: 25% hydrolysis by Ram2
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Lactiplantibacillus plantarum ATCC BAA-793
Substrates: 25% hydrolysis by Ram2
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Lactiplantibacillus plantarum ATCC BAA-793
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Lactiplantibacillus plantarum NCIMB 8826
Substrates: 25% hydrolysis by Ram2
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Lactiplantibacillus plantarum NCIMB 8826
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
F6IEX3
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Talaromyces stollii CLY-6
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: best substrate, molar conversion rate of 99.8%
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: best substrate, molar conversion rate of 99.8%
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
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rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercitrin + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
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rutin + H2O
isoquercitrin + alpha-L-rhamnose
Alternaria alternata SK37.001
-
Substrates: -
Products: -
Products: -
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rutin + H2O
isoquercitrin + alpha-L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercitrin + alpha-L-rhamnose
Substrates: 136.7% of the activity compared to naringin
Products: -
Products: -
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rutin + H2O
isoquercitrin + alpha-L-rhamnose
Aspergillus niger JMU-TS528
Substrates: -
Products: -
Products: -
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rutin + H2O
isoquercitrin + alpha-L-rhamnose
Aspergillus niger JMU-TS528
Substrates: 136.7% of the activity compared to naringin
Products: -
Products: -
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rutin + H2O
isoquercitrin + alpha-L-rhamnose
-
Substrates: 68% of the activity compared to 4-nitrophenyl-alpha-L-rhamnopyranoside
Products: -
Products: -
?
rutin + H2O
isoquercitrin + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercitrin + alpha-L-rhamnose
Substrates: -
Products: -
Products: -
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rutin + H2O
isoquercitrin + alpha-L-rhamnose
Substrates: the yield of isoquercitrin for the wild-type enzyme reached the maximum at 4 h. However, the yield of isoquercitrin for the mutants D594Q and G827K/D594Q enzyme reached the maximum at 6 h. The D594Q and G827K/D594Q mutant enzymes produce 13.5% and 11.0% more isoquercitrin than the wild-type, respectively
Products: -
Products: -
?
rutin + H2O
isoquercitrin + alpha-L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercitrin + alpha-L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercitrin + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
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rutin + H2O
isoquercitrin + alpha-L-rhamnose
Fusarium verticillioides MTCC-2088
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Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercitrin + alpha-L-rhamnose
Substrates: 10.1% relative activity compared to hesperidin
Products: -
Products: -
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rutin + H2O
isoquercitrin + alpha-L-rhamnose
Substrates: isoform RhaB1 exhibits highest activity against rutin
Products: -
Products: -
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rutin + H2O
isoquercitrin + alpha-L-rhamnose
Substrates: 10.1% relative activity compared to hesperidin
Products: -
Products: -
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rutin + H2O
isoquercitrin + alpha-L-rhamnose
Substrates: isoform RhaB1 exhibits highest activity against rutin
Products: -
Products: -
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rutin + H2O
isoquercitrin + alpha-L-rhamnose
F6IEX3
Substrates: -
Products: -
Products: -
?
rutin + H2O
quercetin-3-beta-D-glucoside + L-rhamnose
-
Substrates: -
Products: -
Products: -
?
rutin + H2O
quercetin-3-beta-D-glucoside + L-rhamnose
-
Substrates: low activity
Products: -
Products: -
?
rutin + H2O
quercetin-3-beta-D-glucoside + L-rhamnose
Papiliotrema laurentii ZJU-L07
-
Substrates: -
Products: -
Products: -
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rutinose + H2O
L-rhamnose + D-glucose
Substrates: 6-O-alpha-L-rhamnosyl-D-glucose, Ram1 demonstrates a reduced activity towards rutinose with 4% hydrolysis in 30 min
Products: -
Products: -
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rutinose + H2O
L-rhamnose + D-glucose
Substrates: 6-O-alpha-L-rhamnosyl-D-glucose, 100% hydrolysis by Ram2 at pH 7.0, 31.6 to 35.6% hydrolysis at pH 4.0
Products: -
Products: -
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rutinose + H2O
L-rhamnose + D-glucose
Lactiplantibacillus plantarum ATCC BAA-793
Substrates: 6-O-alpha-L-rhamnosyl-D-glucose, Ram1 demonstrates a reduced activity towards rutinose with 4% hydrolysis in 30 min
Products: -
Products: -
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rutinose + H2O
L-rhamnose + D-glucose
Lactiplantibacillus plantarum ATCC BAA-793
Substrates: 6-O-alpha-L-rhamnosyl-D-glucose, 100% hydrolysis by Ram2 at pH 7.0, 31.6 to 35.6% hydrolysis at pH 4.0
Products: -
Products: -
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rutinose + H2O
L-rhamnose + D-glucose
Lactiplantibacillus plantarum NCIMB 8826
Substrates: 6-O-alpha-L-rhamnosyl-D-glucose, Ram1 demonstrates a reduced activity towards rutinose with 4% hydrolysis in 30 min
Products: -
Products: -
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rutinose + H2O
L-rhamnose + D-glucose
Lactiplantibacillus plantarum NCIMB 8826
Substrates: 6-O-alpha-L-rhamnosyl-D-glucose, 100% hydrolysis by Ram2 at pH 7.0, 31.6 to 35.6% hydrolysis at pH 4.0
Products: -
Products: -
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saikosaponin C + H2O
(3beta,16beta)-16-hydroxy-13,28-epoxyolean-11-en-3-yl) 6-O-beta-D-glucopyranosyl-beta-D-glucopyranoside + alpha-L-rhamnose
Substrates: low activity
Products: -
Products: -
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saikosaponin C + H2O
(3beta,16beta)-16-hydroxy-13,28-epoxyolean-11-en-3-yl) 6-O-beta-D-glucopyranosyl-beta-D-glucopyranoside + alpha-L-rhamnose
Substrates: 9.19% of the activity compared to naringin
Products: -
Products: -
?
saikosaponin C + H2O
? + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
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additional information
?
-
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Substrates: enzyme is able to hydrolyze alpha-1,2- and alpha-1,6-linkages to beta-D-glucosides in addition to direct linkages from the L-rhamnose residue to the aglycon
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme can not hydrolyze ginsenoside Rg2 or saikosaponin C
Products: -
Products: -
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additional information
?
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Substrates: alpha-L-rhamnosidase from Alternaria sp. L1, RhaL1, can catalyze rhamnosylation through reverse hydrolysis reaction. It is used to perform one-step rhamnosylation of anticancer drugs, including 2'-deoxy-5-fluorouridine (FUDR), cytosine arabinoside (Ara C), and hydroxyurea (Hydrea). Maximum yields of each rhamnosylated drugs are 57.7 mmol for rhamnosylated Ara C, 68.6 mmol for rhamnosylated Hydrea, and 42.2 mmol for rhamnosylated FUDR. The rhamnosylated drugs exhibit little cytotoxic effects on cancer cells, but efficiently restore cytotoxic activity when incubated with exogenous alpha-L-rhamnosidase, allowing their potential applications in the enzyme-activated prodrug system. Method optimization, product identification by NMR analysis, overview
Products: -
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additional information
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Substrates: no substrate: quercitrin
Products: -
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additional information
?
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Substrates: no substrate: quercitrin
Products: -
Products: -
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additional information
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-
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Substrates: no substrate: quercitrin
Products: -
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additional information
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-
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Substrates: RhaA and RhaB selectively remove terminal alpha-L-rhamnosyl groups in situ in orange juice, blackcurrant juice, and green tea infusion resulting in a decrease of flavonoid rutinosides, i.e. anthocyanins, flavanones, and flavonols, respectively, and concomitant increase in their flavonoid glucoside counterparts, product identification and quantification by HPLC-MS, overview
Products: -
Products: -
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additional information
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Substrates: RhaA and RhaB selectively remove terminal alpha-L-rhamnosyl groups in situ in orange juice, blackcurrant juice, and green tea infusion resulting in a decrease of flavonoid rutinosides, i.e. anthocyanins, flavanones, and flavonols, respectively, and concomitant increase in their flavonoid glucoside counterparts, product identification and quantification by HPLC-MS, overview
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Products: -
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additional information
?
-
Substrates: enzyme is able to hydrolyze alpha-(1-2) amd alpha-(1-6) glycosidic bonds
Products: -
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additional information
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-
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Substrates: acts both on alpha-1,2- and on alpha-1,6-linkages
Products: -
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additional information
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Substrates: the enzyme posseses broad substrate specificities by hydrolyzing alpha-1,2, alpha-1,3 alpha-1,4, and alpha-1,6 linkages to beta-D-glucosides
Products: -
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additional information
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Substrates: recombinant alpha-L-rhamnosidase N12-Rha has significantly higher catalytic activity on alpha-1,6 glycosidic bond than alpha-1,2 glycosidic bond, and has no activity on alpha-1,3 glycosidic bond. The activities with hesperidin and naringin are 7240 U/ml and 945 U/ml, respectively, which are 10.63 times that of native alpha-L-rhamnosidase
Products: -
Products: -
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additional information
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Substrates: rutin is the most suitable substrate for Rha-N1 compared to hesperidin and naringin
Products: -
Products: -
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additional information
?
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Substrates: alpha-L-rhamnosidase hydrolyzes alpha-1,2 and alpha-1,6-glycosidic bonds in naringin and rutin, respectively, thus generating prunin and isoquercitrin, respectively
Products: -
Products: -
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additional information
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Aspergillus niger CCTCC M 2018240
Substrates: alpha-L-rhamnosidase hydrolyzes alpha-1,2 and alpha-1,6-glycosidic bonds in naringin and rutin, respectively, thus generating prunin and isoquercitrin, respectively
Products: -
Products: -
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additional information
?
-
-
Substrates: no activity with myricetrin
Products: -
Products: -
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additional information
?
-
-
Substrates: the specific activity of the recombinant wild-type enzyme AoRhaA is higher toward hesperidin and narirutin, where the L-rhamnose residue is alpha-1,6-linked to beta-D-glucoside, than toward neohesperidin and naringin with an alpha-1,2-linkage to beta-D-glucoside. No activity is detected toward quercitrin, myricitrin, and epimedin C
Products: -
Products: -
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additional information
?
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Aspergillus oryzae NL-1
-
Substrates: no activity with myricetrin
Products: -
Products: -
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additional information
?
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Substrates: AtRha and beta-glucosidase TthBg3 show excellent selectivity to cleave the rhamnose at the 3rd position and the glucosyl at the C-7 group of icariin, which establishes an effective and green method to produce the more pharmacological active icaritin. Method optimization, overview. After a two-stage transformation under optimized conditions, 0.5 g/l of icariin is transformed into 0.25 g/l of icaritin, with a corresponding molar conversion rate of 91.2%
Products: -
Products: -
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additional information
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Aspergillus terreus CCF3059
Substrates: AtRha and beta-glucosidase TthBg3 show excellent selectivity to cleave the rhamnose at the 3rd position and the glucosyl at the C-7 group of icariin, which establishes an effective and green method to produce the more pharmacological active icaritin. Method optimization, overview. After a two-stage transformation under optimized conditions, 0.5 g/l of icariin is transformed into 0.25 g/l of icaritin, with a corresponding molar conversion rate of 91.2%
Products: -
Products: -
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additional information
?
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Q93RE8
Substrates: isozyme plays a crucial role in complete metabolism of gellan
Products: -
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additional information
?
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Q93RE7
Substrates: isozyme plays a crucial role in complete metabolism of gellan
Products: -
Products: -
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additional information
?
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Q93RE8
Substrates: isozyme plays a crucial role in complete metabolism of gellan
Products: -
Products: -
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additional information
?
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Q93RE7
Substrates: isozyme plays a crucial role in complete metabolism of gellan
Products: -
Products: -
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additional information
?
-
Substrates: no the enzyme exhibits high selectivity to cleave the alpha-1,2 and alpha-1,6 glycosidic bond between rhamnoside and rhamnoside, rhamnoside and glycoside
Products: -
Products: -
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additional information
?
-
-
Substrates: no the enzyme exhibits high selectivity to cleave the alpha-1,2 and alpha-1,6 glycosidic bond between rhamnoside and rhamnoside, rhamnoside and glycoside
Products: -
Products: -
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additional information
?
-
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Substrates: enzyme BtRha converts epimedin B, sagittatoside B, and notoginsenoside R1, but BtRha does not transform astragaloside A and icariin
Products: -
Products: -
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additional information
?
-
Substrates: no the enzyme exhibits high selectivity to cleave the alpha-1,2 and alpha-1,6 glycosidic bond between rhamnoside and rhamnoside, rhamnoside and glycoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: no the enzyme exhibits high selectivity to cleave the alpha-1,2 and alpha-1,6 glycosidic bond between rhamnoside and rhamnoside, rhamnoside and glycoside
Products: -
Products: -
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additional information
?
-
Substrates: the specific activity of the enzyme with aryl-glycoside substrates follows the descending order 4-nitrophenyl alpha-L-rhamnopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl beta-D-galactopyranoside, and 2-nitrophenyl alpha-D-glucopyranoside. Substrate specificity, overview. No hydrolysis activity of the enzyme with prunin, isoquercetin, and hesperetin-7-O-glucoside. Also no activity with 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-beta-D-xylopyranoside, 4-nitrophenyl-beta-D-mannopyranoside, and 2-nitrophenyl-beta-D-xylopyranoside. The enzyme exhibits higher activity for a-1,6 linkage (rutin and hesperidin) than for a-1,2 linkage (naringin)
Products: -
Products: -
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additional information
?
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Substrates: the specific activity of the enzyme with aryl-glycoside substrates follows the descending order 4-nitrophenyl alpha-L-rhamnopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl beta-D-galactopyranoside, and 2-nitrophenyl alpha-D-glucopyranoside. Substrate specificity, overview. No hydrolysis activity of the enzyme with prunin, isoquercetin, and hesperetin-7-O-glucoside. Also no activity with 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-beta-D-xylopyranoside, 4-nitrophenyl-beta-D-mannopyranoside, and 2-nitrophenyl-beta-D-xylopyranoside. The enzyme exhibits higher activity for a-1,6 linkage (rutin and hesperidin) than for a-1,2 linkage (naringin)
Products: -
Products: -
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additional information
?
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Substrates: the specific activity of the enzyme with aryl-glycoside substrates follows the descending order 4-nitrophenyl alpha-L-rhamnopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl beta-D-galactopyranoside, and 2-nitrophenyl alpha-D-glucopyranoside. Substrate specificity, overview. No hydrolysis activity of the enzyme with prunin, isoquercetin, and hesperetin-7-O-glucoside. Also no activity with 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-beta-D-xylopyranoside, 4-nitrophenyl-beta-D-mannopyranoside, and 2-nitrophenyl-beta-D-xylopyranoside. The enzyme exhibits higher activity for a-1,6 linkage (rutin and hesperidin) than for a-1,2 linkage (naringin)
Products: -
Products: -
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additional information
?
-
Substrates: the specific activity of the enzyme with aryl-glycoside substrates follows the descending order 4-nitrophenyl alpha-L-rhamnopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl beta-D-galactopyranoside, and 2-nitrophenyl alpha-D-glucopyranoside. Substrate specificity, overview. No hydrolysis activity of the enzyme with prunin, isoquercetin, and hesperetin-7-O-glucoside. Also no activity with 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-beta-D-xylopyranoside, 4-nitrophenyl-beta-D-mannopyranoside, and 2-nitrophenyl-beta-D-xylopyranoside. The enzyme exhibits higher activity for a-1,6 linkage (rutin and hesperidin) than for a-1,2 linkage (naringin)
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additional information
?
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Substrates: no activity is detected towards the alpha-1,2 linkage in naringin
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Products: -
?
additional information
?
-
Substrates: no activity is detected towards the alpha-1,2 linkage in naringin
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?
additional information
?
-
-
Substrates: no activity is detected towards the alpha-1,2 linkage in naringin
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?
additional information
?
-
Substrates: no activity towards quercitin, gellan gum, vitexin 2-O-rhamnoside, and alpha-chaconine
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?
additional information
?
-
Substrates: no activity towards quercitin, gellan gum, vitexin 2-O-rhamnoside, and alpha-chaconine
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Products: -
?
additional information
?
-
-
Substrates: no activity towards quercitin, gellan gum, vitexin 2-O-rhamnoside, and alpha-chaconine
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Products: -
?
additional information
?
-
Substrates: substrate specificity analysis of enzyme Ram1 towards the disaccharide rutinose and natural dietary flavonoids naringin and rutin and comparison to that of isozyme Ram2 from Lactobacillus plantarum and to a commercial multienzyme complex, PPO, which efficiently converted both naringin and rutin into their corresponding aglycones, overview. Isozyme Ram1 is a less acidic- and heat-active enzyme than isozyme Ram2 and exhibits a high activity towards 4-nitrophenyl-alpha-L-rhamnopyranoside, but it is unable to hydrolyze neither rutinose, naringin, or rutin. In contrast, isozyme Ram2 shows a substrate specificity towards alpha-(1->6) glycosidic flavonoids, such as rutin, and the disaccharide rutinose. Ram1 also shows low additional activities towards 4-nitrophenyl-alpha-L-arabinopyranoside and 4-nitrophenyl-beta-D-galactopyranoside. Low activity with rutinose
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Products: -
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additional information
?
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Substrates: substrate specificity analysis of enzyme Ram1 towards the disaccharide rutinose and natural dietary flavonoids naringin and rutin and comparison to that of isozyme Ram2 from Lactobacillus plantarum and to a commercial multienzyme complex, PPO, which efficiently converted both naringin and rutin into their corresponding aglycones, overview. Isozyme Ram1 is a less acidic- and heat-active enzyme than isozyme Ram2 and exhibits a high activity towards 4-nitrophenyl-alpha-L-rhamnopyranoside, but it is unable to hydrolyze neither rutinose, naringin, or rutin. In contrast, isozyme Ram2 shows a substrate specificity towards alpha-(1->6) glycosidic flavonoids, such as rutin, and the disaccharide rutinose. Ram1 also shows low additional activities towards 4-nitrophenyl-alpha-L-arabinopyranoside and 4-nitrophenyl-beta-D-galactopyranoside. Low activity with rutinose
Products: -
Products: -
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additional information
?
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Substrates: substrate specificity analysis of enzyme Ram2 towards the disaccharide rutinose and natural dietary flavonoids naringin and rutin and comparison to that of isozyme Ram1 from Lactobacillus plantarum and to a commercial multienzyme complex, PPO, which efficiently converts both naringin and rutin into their corresponding aglycones, overview. Isozyme Ram1 is a less acidic- and heat-active enzyme than isozyme Ram2 and exhibits a high activity towards 4-nitrophenyl-alpha-L-rhamnopyranoside, but it is unable to hydrolyze neither rutinose, naringin or rutin. In contrast, isozyme Ram2 shows a substrate specificity towards alpha-(1->6) glycosidic flavonoids, such as rutin, and the disaccharide rutinose. The mechanism of action of Ram2 towards rutin is elucidated and reveals the potential cost-effective and selective production of the monoglycosylated flavonoid isoquercetin (quercetin-3-O-glucoside). Poor activity with naringin by Ram2
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additional information
?
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Substrates: substrate specificity analysis of enzyme Ram2 towards the disaccharide rutinose and natural dietary flavonoids naringin and rutin and comparison to that of isozyme Ram1 from Lactobacillus plantarum and to a commercial multienzyme complex, PPO, which efficiently converts both naringin and rutin into their corresponding aglycones, overview. Isozyme Ram1 is a less acidic- and heat-active enzyme than isozyme Ram2 and exhibits a high activity towards 4-nitrophenyl-alpha-L-rhamnopyranoside, but it is unable to hydrolyze neither rutinose, naringin or rutin. In contrast, isozyme Ram2 shows a substrate specificity towards alpha-(1->6) glycosidic flavonoids, such as rutin, and the disaccharide rutinose. The mechanism of action of Ram2 towards rutin is elucidated and reveals the potential cost-effective and selective production of the monoglycosylated flavonoid isoquercetin (quercetin-3-O-glucoside). Poor activity with naringin by Ram2
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additional information
?
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Lactiplantibacillus plantarum ATCC BAA-793
Substrates: substrate specificity analysis of enzyme Ram1 towards the disaccharide rutinose and natural dietary flavonoids naringin and rutin and comparison to that of isozyme Ram2 from Lactobacillus plantarum and to a commercial multienzyme complex, PPO, which efficiently converted both naringin and rutin into their corresponding aglycones, overview. Isozyme Ram1 is a less acidic- and heat-active enzyme than isozyme Ram2 and exhibits a high activity towards 4-nitrophenyl-alpha-L-rhamnopyranoside, but it is unable to hydrolyze neither rutinose, naringin, or rutin. In contrast, isozyme Ram2 shows a substrate specificity towards alpha-(1->6) glycosidic flavonoids, such as rutin, and the disaccharide rutinose. Ram1 also shows low additional activities towards 4-nitrophenyl-alpha-L-arabinopyranoside and 4-nitrophenyl-beta-D-galactopyranoside. Low activity with rutinose
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additional information
?
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Lactiplantibacillus plantarum ATCC BAA-793
Substrates: substrate specificity analysis of enzyme Ram1 towards the disaccharide rutinose and natural dietary flavonoids naringin and rutin and comparison to that of isozyme Ram2 from Lactobacillus plantarum and to a commercial multienzyme complex, PPO, which efficiently converted both naringin and rutin into their corresponding aglycones, overview. Isozyme Ram1 is a less acidic- and heat-active enzyme than isozyme Ram2 and exhibits a high activity towards 4-nitrophenyl-alpha-L-rhamnopyranoside, but it is unable to hydrolyze neither rutinose, naringin, or rutin. In contrast, isozyme Ram2 shows a substrate specificity towards alpha-(1->6) glycosidic flavonoids, such as rutin, and the disaccharide rutinose. Ram1 also shows low additional activities towards 4-nitrophenyl-alpha-L-arabinopyranoside and 4-nitrophenyl-beta-D-galactopyranoside. Low activity with rutinose
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additional information
?
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Lactiplantibacillus plantarum ATCC BAA-793
Substrates: substrate specificity analysis of enzyme Ram2 towards the disaccharide rutinose and natural dietary flavonoids naringin and rutin and comparison to that of isozyme Ram1 from Lactobacillus plantarum and to a commercial multienzyme complex, PPO, which efficiently converts both naringin and rutin into their corresponding aglycones, overview. Isozyme Ram1 is a less acidic- and heat-active enzyme than isozyme Ram2 and exhibits a high activity towards 4-nitrophenyl-alpha-L-rhamnopyranoside, but it is unable to hydrolyze neither rutinose, naringin or rutin. In contrast, isozyme Ram2 shows a substrate specificity towards alpha-(1->6) glycosidic flavonoids, such as rutin, and the disaccharide rutinose. The mechanism of action of Ram2 towards rutin is elucidated and reveals the potential cost-effective and selective production of the monoglycosylated flavonoid isoquercetin (quercetin-3-O-glucoside). Poor activity with naringin by Ram2
Products: -
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additional information
?
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Lactiplantibacillus plantarum ATCC BAA-793
Substrates: substrate specificity analysis of enzyme Ram2 towards the disaccharide rutinose and natural dietary flavonoids naringin and rutin and comparison to that of isozyme Ram1 from Lactobacillus plantarum and to a commercial multienzyme complex, PPO, which efficiently converts both naringin and rutin into their corresponding aglycones, overview. Isozyme Ram1 is a less acidic- and heat-active enzyme than isozyme Ram2 and exhibits a high activity towards 4-nitrophenyl-alpha-L-rhamnopyranoside, but it is unable to hydrolyze neither rutinose, naringin or rutin. In contrast, isozyme Ram2 shows a substrate specificity towards alpha-(1->6) glycosidic flavonoids, such as rutin, and the disaccharide rutinose. The mechanism of action of Ram2 towards rutin is elucidated and reveals the potential cost-effective and selective production of the monoglycosylated flavonoid isoquercetin (quercetin-3-O-glucoside). Poor activity with naringin by Ram2
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-
additional information
?
-
Substrates: no activity is detected towards the alpha-1,2 linkage in naringin
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?
additional information
?
-
Substrates: no activity is detected towards the alpha-1,2 linkage in naringin
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?
additional information
?
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Lactiplantibacillus plantarum NCIMB 8826
Substrates: substrate specificity analysis of enzyme Ram1 towards the disaccharide rutinose and natural dietary flavonoids naringin and rutin and comparison to that of isozyme Ram2 from Lactobacillus plantarum and to a commercial multienzyme complex, PPO, which efficiently converted both naringin and rutin into their corresponding aglycones, overview. Isozyme Ram1 is a less acidic- and heat-active enzyme than isozyme Ram2 and exhibits a high activity towards 4-nitrophenyl-alpha-L-rhamnopyranoside, but it is unable to hydrolyze neither rutinose, naringin, or rutin. In contrast, isozyme Ram2 shows a substrate specificity towards alpha-(1->6) glycosidic flavonoids, such as rutin, and the disaccharide rutinose. Ram1 also shows low additional activities towards 4-nitrophenyl-alpha-L-arabinopyranoside and 4-nitrophenyl-beta-D-galactopyranoside. Low activity with rutinose
Products: -
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additional information
?
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Lactiplantibacillus plantarum NCIMB 8826
Substrates: substrate specificity analysis of enzyme Ram1 towards the disaccharide rutinose and natural dietary flavonoids naringin and rutin and comparison to that of isozyme Ram2 from Lactobacillus plantarum and to a commercial multienzyme complex, PPO, which efficiently converted both naringin and rutin into their corresponding aglycones, overview. Isozyme Ram1 is a less acidic- and heat-active enzyme than isozyme Ram2 and exhibits a high activity towards 4-nitrophenyl-alpha-L-rhamnopyranoside, but it is unable to hydrolyze neither rutinose, naringin, or rutin. In contrast, isozyme Ram2 shows a substrate specificity towards alpha-(1->6) glycosidic flavonoids, such as rutin, and the disaccharide rutinose. Ram1 also shows low additional activities towards 4-nitrophenyl-alpha-L-arabinopyranoside and 4-nitrophenyl-beta-D-galactopyranoside. Low activity with rutinose
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Products: -
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additional information
?
-
Lactiplantibacillus plantarum NCIMB 8826
Substrates: substrate specificity analysis of enzyme Ram2 towards the disaccharide rutinose and natural dietary flavonoids naringin and rutin and comparison to that of isozyme Ram1 from Lactobacillus plantarum and to a commercial multienzyme complex, PPO, which efficiently converts both naringin and rutin into their corresponding aglycones, overview. Isozyme Ram1 is a less acidic- and heat-active enzyme than isozyme Ram2 and exhibits a high activity towards 4-nitrophenyl-alpha-L-rhamnopyranoside, but it is unable to hydrolyze neither rutinose, naringin or rutin. In contrast, isozyme Ram2 shows a substrate specificity towards alpha-(1->6) glycosidic flavonoids, such as rutin, and the disaccharide rutinose. The mechanism of action of Ram2 towards rutin is elucidated and reveals the potential cost-effective and selective production of the monoglycosylated flavonoid isoquercetin (quercetin-3-O-glucoside). Poor activity with naringin by Ram2
Products: -
Products: -
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additional information
?
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Lactiplantibacillus plantarum NCIMB 8826
Substrates: substrate specificity analysis of enzyme Ram2 towards the disaccharide rutinose and natural dietary flavonoids naringin and rutin and comparison to that of isozyme Ram1 from Lactobacillus plantarum and to a commercial multienzyme complex, PPO, which efficiently converts both naringin and rutin into their corresponding aglycones, overview. Isozyme Ram1 is a less acidic- and heat-active enzyme than isozyme Ram2 and exhibits a high activity towards 4-nitrophenyl-alpha-L-rhamnopyranoside, but it is unable to hydrolyze neither rutinose, naringin or rutin. In contrast, isozyme Ram2 shows a substrate specificity towards alpha-(1->6) glycosidic flavonoids, such as rutin, and the disaccharide rutinose. The mechanism of action of Ram2 towards rutin is elucidated and reveals the potential cost-effective and selective production of the monoglycosylated flavonoid isoquercetin (quercetin-3-O-glucoside). Poor activity with naringin by Ram2
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additional information
?
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Substrates: alpha-L-rhamnosidase catalyzes hydrolysis of the terminal non-reducing alpha-L-rhamnosyl residues from a large number of natural rhamnoglycosides including naringin, rutin, diosgene, hesperidin, terpenyl glycosides
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additional information
?
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Substrates: alpha-L-rhamnosidase catalyzes hydrolysis of the terminal non-reducing alpha-L-rhamnosyl residues from a large number of natural rhamnoglycosides including naringin, rutin, diosgene, hesperidin, terpenyl glycosides
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additional information
?
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Substrates: alpha-L-rhamnosidase catalyzes hydrolysis of the terminal non-reducing alpha-L-rhamnosyl residues from a large number of natural rhamnoglycosides including naringin, rutin, diosgene, hesperidin, terpenyl glycosides
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additional information
?
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Substrates: alpha-L-rhamnosidase catalyzes hydrolysis of the terminal non-reducing alpha-L-rhamnosyl residues from a large number of natural rhamnoglycosides including naringin, rutin, diosgene, hesperidin, terpenyl glycosides
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additional information
?
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Substrates: alpha-L-rhamnosidase catalyzes hydrolysis of the terminal non-reducing alpha-L-rhamnosyl residues from a large number of natural rhamnoglycosides including naringin, rutin, diosgene, hesperidin, terpenyl glycosides
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additional information
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F6IEX3
Substrates: the enzyme is able to hydrolyze rhamnose from natural flavonoids. It hydrolyzes both alpha-1,2 and alpha-1,6 glycosidic linkages
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?
additional information
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-
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Substrates: RHA-P is a catalytically efficient, thermostable alpha-L-rhamnosidase that selectively hydrolyzes alpha-1,6 and alpha-1,2 glycosidiclinkages between a terminal rhamnose and a flavonoid moiety. Substrate docking study including compound L-rhamnose-alpha-1,2-L-arabinopyranose-alpha-1,4-D-galactose-beta-2,1-L-aceric acid-alpha-3,1-L-rhanose-alpha-3,1-D-apiose, overview. No binding of the enzyme with rutinose, rhamnose, and neohesperidose. RHA-P is a promiscuous enzyme, all of the docked substrates hydrogen bond to one or more residues of the DRW triad, a hydrogen bonding network in RHA-P involving D587, R619, and W610
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additional information
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Substrates: besides cleaving the binding between L-rhamnose and aglycon, the enzyme can also cleave the alpha-1,2 glycosidic linkage between glucoside and rhamnoside in naringin and neohesperidin. The enzyme prefers the celavage of alpha-1,2-linkages compared to alpha-1,6-linkages
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additional information
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-
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Substrates: the enzyme shows no activity toward synthetic substrates with beta-linked carbohydrates (4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl beta-N-acetylglucosaminide), which indicates the ability to derhamnosylate plant flavonoids, but not completely deglycosylate them. The enzyme is highly selective for terminal alpha-1,2-linked rhamnose
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additional information
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Substrates: enzyme TstRhaA can hydrolyze natural products containing alpha-1,2 and alpha-1,6 glycosidic bonds but not alpha-1 glycosidic bond natural products. No activity with myricetrin and with pNPGlu, pNPArf, pNPArp, pNPGal, or pNPXyl
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additional information
?
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Substrates: no activity with quercitrin
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?
additional information
?
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Substrates: no activity with quercitrin
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?
additional information
?
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Substrates: no activity with rutin and quercitrin
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?
additional information
?
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Substrates: no activity with rutin and quercitrin
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
gypenoside-5 + H2O
ginsenoside Rd + alpha-L-rhamnose
-
Substrates: -
Products: -
Products: -
?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
Bacteroides JY-6
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
-
Substrates: alpha-L-rhamnose in glycolipids or glycosides
Products: -
Products: -
?
epoetin C + H2O
icariin + L-rhamnose
-
Substrates: -
Products: -
Products: -
?
epoetin C + H2O
icariin + L-rhamnose
-
Substrates: -
Products: -
Products: -
?
gellan + H2O
alpha-L-rhamnose + ?
Q93RE7
Substrates: hydrolytic reaction, release of rhamnose from the disaccharide
Products: -
Products: -
?
gellan + H2O
alpha-L-rhamnose + ?
Q93RE7
Substrates: hydrolytic reaction, release of rhamnose from the disaccharide
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Aspergillus niger ATCC MYA-4892
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Aspergillus niger CCTCC M 2018240
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Aspergillus niger FGSC A1513
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Aspergillus niger JMU-TS528
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Q93RE8, Q93RE7
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Bacteroides thetaiotaomicron CCUG 10774
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Bacteroides thetaiotaomicron JCM 5827
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Klebsiella oxytoca BUCSAV 143
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Klebsiella oxytoca CCM 1901
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Lactiplantibacillus plantarum ATCC BAA-793
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Lactiplantibacillus plantarum NCIMB 8826
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
F6IEX3
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Papiliotrema laurentii ZJU-L07
-
Substrates: -
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Talaromyces stollii CLY-6
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
hesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
naringin + H2O
? + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Aspergillus niger CCTCC M 2018240
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Aspergillus niger JMU-TS528
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Q93RE8, Q93RE7
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Bacteroides thetaiotaomicron CCUG 10774
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Bacteroides thetaiotaomicron JCM 5827
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Klebsiella oxytoca BUCSAV 143
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Klebsiella oxytoca CCM 1901
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Lactiplantibacillus plantarum ATCC BAA-793
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Lactiplantibacillus plantarum NCIMB 8826
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: -
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
F6IEX3
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Talaromyces stollii CLY-6
-
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
naringin + H2O
prunin + L-rhamnose
Substrates: hydrolysis of an alpha-1,2-bond
Products: -
Products: -
?
neohesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
-
Substrates: -
Products: -
Products: -
?
neohesperidin + H2O
hesperetin-7-O-glucoside + L-rhamnose
Papiliotrema laurentii ZJU-L07
-
Substrates: -
Products: -
Products: -
?
quercitrin + H2O
quercetin + L-rhamnose
-
Substrates: quercitrin is identical with quercetin 3-L-rhamnoside, growth on quercitrin as carbon source
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Aspergillus niger CCTCC M 2018240
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Aspergillus niger JMU-TS528
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Q93RE8, Q93RE7
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Bacteroides thetaiotaomicron CCUG 10774
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Bacteroides thetaiotaomicron JCM 5827
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Klebsiella oxytoca BUCSAV 143
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Klebsiella oxytoca CCM 1901
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Lactiplantibacillus plantarum ATCC BAA-793
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Lactiplantibacillus plantarum NCIMB 8826
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
F6IEX3
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Talaromyces stollii CLY-6
-
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: -
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
R4P072
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
isoquercetin + L-rhamnose
Substrates: hydrolysis of an alpha-1,6-bond
Products: -
Products: -
?
rutin + H2O
quercetin-3-beta-D-glucoside + L-rhamnose
-
Substrates: -
Products: -
Products: -
?
rutin + H2O
quercetin-3-beta-D-glucoside + L-rhamnose
Papiliotrema laurentii ZJU-L07
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Q93RE8
Substrates: isozyme plays a crucial role in complete metabolism of gellan
Products: -
Products: -
?
additional information
?
-
Q93RE7
Substrates: isozyme plays a crucial role in complete metabolism of gellan
Products: -
Products: -
?
additional information
?
-
Q93RE8
Substrates: isozyme plays a crucial role in complete metabolism of gellan
Products: -
Products: -
?
additional information
?
-
Q93RE7
Substrates: isozyme plays a crucial role in complete metabolism of gellan
Products: -
Products: -
?
additional information
?
-
Substrates: alpha-L-rhamnosidase catalyzes hydrolysis of the terminal non-reducing alpha-L-rhamnosyl residues from a large number of natural rhamnoglycosides including naringin, rutin, diosgene, hesperidin, terpenyl glycosides
Products: -
Products: -
-
additional information
?
-
Substrates: alpha-L-rhamnosidase catalyzes hydrolysis of the terminal non-reducing alpha-L-rhamnosyl residues from a large number of natural rhamnoglycosides including naringin, rutin, diosgene, hesperidin, terpenyl glycosides
Products: -
Products: -
-
additional information
?
-
Substrates: alpha-L-rhamnosidase catalyzes hydrolysis of the terminal non-reducing alpha-L-rhamnosyl residues from a large number of natural rhamnoglycosides including naringin, rutin, diosgene, hesperidin, terpenyl glycosides
Products: -
Products: -
-
additional information
?
-
Substrates: alpha-L-rhamnosidase catalyzes hydrolysis of the terminal non-reducing alpha-L-rhamnosyl residues from a large number of natural rhamnoglycosides including naringin, rutin, diosgene, hesperidin, terpenyl glycosides
Products: -
Products: -
-
additional information
?
-
Substrates: alpha-L-rhamnosidase catalyzes hydrolysis of the terminal non-reducing alpha-L-rhamnosyl residues from a large number of natural rhamnoglycosides including naringin, rutin, diosgene, hesperidin, terpenyl glycosides
Products: -
Products: -
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Al3+
Ba2+
Ca2+
Co2+
Fe2+
Fe3+
Li+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Ca2+
Q93RE7
calcium ions essential for crystallization, calcium binding shown in crystallized form
Ca2+
F6IEX3
EDTA-treated enzyme recovers its activity in the presence of divalent cations such as Mg2+ and Ca2+, but with an apparent higher efficiency when calcium is used. Almost total recovery of activity in the presence of a 3000-fold excess of Ca2+ compared to the 56% obtained with a similar excess of Mg2+. Five residues contribute to the binding of the Ca2+ ion: E593, E538, D458, S459 and E561
Mg2+
F6IEX3
EDTA-treated enzyme recovers its activity in the presence of divalent cations such as Mg2+ and Ca2+, but with an apparent higher efficiency when calcium is used. Almost total recovery of activity in the presence of a 3000-fold excess of Ca2+ compared to the 56% obtained with a similar excess of Mg2+
additional information
K+, Na+, Ca2+, Ni2+, Co2+, and Mn2+ at the concentrations of 1 mM, 10 mM, 50 mM, 100 mM, and 150 mM have little effect on the enzyme activity of engineered recombinant enzyme N12-Rha
additional information
EDTA and DTT have almost no effect on the enzymatic activity of AtRha. And metal ions have no effect on the catalytic and 3D structure of the enzyme
additional information
no significant effects on enzyme activity by 1 mM of Na+, Ca2+, K+, and NH4+
additional information
-
poor effects on enzyme activity by 0.2 mM of Mn2+, Co2+, K+, and Ba2+, no effects by 0.2 mM of Al3+ and Ni2+
additional information
no significant effects on enzyme activity by 1 mM of Na+, Ca2+, K+, and NH4+
additional information
no effect by EDTA, Zn2+, Mg2+, Ca2+, and Mn2+ on RhmA
additional information
no effect by EDTA, Zn2+, Mg2+, Ca2+, and Mn2+ on RhmA
additional information
no effect by EDTA, Mg2+, Ca2+, and Mn2+ on RhmB
additional information
no effect by EDTA, Mg2+, Ca2+, and Mn2+ on RhmB
additional information
R4P072
no significant effects on enzyme activity by 1 mM of Na+, Ca2+, K+, and NH4+
additional information
no significant effects on enzyme activity by 1 mM of Na+, Ca2+, K+, and NH4+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3S,4S)-3,4-dihydroxy-5-spirocyclopropyl-DELTA-pyrroline
-
72% inhibition at 1 mM
1,10-phenanthroline
less effective inhibitor, when the 1,10-phenanthroline concentration is raised to 10 mM, the activity of isoform RhaB1 decreases by 50%; less effective inhibitor, when the 1,10-phenanthroline concentration is raised to 10 mM, the activity of isoform RhaB2 decreases by 50%
1-(3-dimethylaminopropyl)-3-ethylcarbodiimide methiodide
-
60% inhibition at 10 mM
-
acetonitrile
1% (v/v), about 55% loss of activity, 5% (v/v), about 90% loss of activity
dimethyl sulfoxide
the addition of organic solvent can enhance solubility of naringin dihydrochalcone, but it also decreases enzyme activity. Dimethyl sulfoxide, acetone and methanol decrease enzyme activity more seriously than that of ethanol. When necessary, ethanol as a co-solvent with quantity less than 5% (v/v) is ecommended to improve the hydrolysis reaction of naringin dihydrochalcone
DMSO
1% (v/v), about 45% loss of activity, 5% (v/v), about 75% loss of activity
ethylene glycol
1% (v/v), about 15% loss of activity, 5% (v/v), about 30% loss of activity
five-membered ring azasugars
-
with L-rhamnose configuration, substitution at the nitrogen shifts the inhibition mechanism from mixed to competitive
-
Isopropanol
1% (v/v), about 25% loss of activity, 5% (v/v), about 55% loss of activity
N,N-Dimethylformamide
1% (v/v), about 70% loss of activity, 5% (v/v), about 90% loss of activity
p-chloromercuribenzoic acid
Q93RE8, Q93RE7
0.1 mM, 50% residual activity
phosphoramidon
isoform RhaB1 shows 23.8% residual activity at 1 mM; isoform RhaB2 shows 42.5% residual activity at 1 mM
polyhexamethylene biguanide
1 mM reduces the activity of isoform RhaB1 to 10.9% and isoform RhaB2 to 36.0% residual activity; 1 mM reduces the activity of isoform RhaB1 to 10.9% residual activity
thiorphan
less effective inhibitor; less effective inhibitor
[4-([[(2S,3S,4R)-3,4-dihydroxypyrrolidin-2-yl]methyl]amino)-5-hydroxy-6-methylpyridin-2-yl]methyl dihydrogen phosphate
-
-
[4-([[(2S,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl]amino)-5-hydroxy-6-methylpyridin-2-yl]methyl dihydrogen phosphate
-
-
acetone
the addition of organic solvent can enhance solubility of naringin dihydrochalcone, but it also decreases enzyme activity. Dimethyl sulfoxide, acetone and methanol decrease enzyme activity more seriously than that of ethanol. When necessary, ethanol as a co-solvent with quantity less than 5% (v/v) is ecommended to improve the hydrolysis reaction of naringin dihydrochalcone
acetone
1% (v/v), about 50% loss of activity, 5% (v/v), about 75% loss of activity
Cu2+
-
activates 1.4fold at 20 mM, inhibits completely at 100 mM
Cu2+
5 mM, 92% loss of activity. 1 mM, 83% loss of activity
CuCl2
Q93RE8, Q93RE7
1 mM, 4% residual activity; 1 mM, 70% residual activity
D-glucose
about 500 mM D-glucose concentration in grape juice inhibits RhmA by 39%; about 500 mM D-glucose concentration in grape juice inhibits RhmB by 38%
ethanol
1% (v/v), about 25% loss of activity, 5% (v/v), about 55% loss of activity
ethanol
at 12% v/v, 51% inhibition of RhmB; at 12% v/v, 60% inhibition of RhmA
Fe3+
-
activates 1.4fold at 10 mM, inhibits completely at 50 mM
L-rhamnose
Q93RE8, Q93RE7
10 mM, 14% residual activity; 10 mM, 37% residual activity
L-rhamnose
Q93RE7
crystallized complex with interacting site determined, for kinetic assay different concentrations ranging between 0 and 100 mM of rhamnose used
L-rhamnose
isoform RhaB1 is slightly inhibited by L-rhamnose, showing noncompetitive inhibition
L-rhamnose
complete inhibition, competitive product inhibition; complete inhibition, competitive product inhibition
methanol
the addition of organic solvent can enhance solubility of naringin dihydrochalcone, but it also decreases enzyme activity. Dimethyl sulfoxide, acetone and methanol decrease enzyme activity more seriously than that of ethanol. When necessary, ethanol as a co-solvent with quantity less than 5% (v/v) is recommended to improve the hydrolysis reaction of naringin dihydrochalcone
methanol
1% (v/v), about 15% loss of activity, 5% (v/v), about 50% loss of activity
SDS
SDS produces partial inactivation; SDS produces partial inactivation
Zn2+
5 mM, 32% loss of activity. 1 mM, 55% loss of activity
Zn2+
30-35% inhibition at 2 mM, reversible by 10 mM EDTA
additional information
-
neither divalent cations such as Ca2+, Mg2+, Mn2+, and Co2+ nor reducing agents such as 2-mercaptoethanol and dithiothreitol show effects on enzyme activtiy
-
additional information
dithiothreitol and beta-mercaptoethanol have no or little effect on activity; dithiothreitol and beta-mercaptoethanol have no or little effect on activity
-
additional information
dithiothreitol and beta-mercaptoethanol have no or little effect on activity; dithiothreitol and beta-mercaptoethanol have no or little effect on activity
-
additional information
-
dithiothreitol and beta-mercaptoethanol have no or little effect on activity; dithiothreitol and beta-mercaptoethanol have no or little effect on activity
-
additional information
-
not inhibitory at 1 mM: EDTA, CaCl2, 2-mercaptoethanol
-
additional information
-
design from aromatic amino acids and inhibitory potency of polyhydroxylated pyrrolidines, stereochemistry, overview
-
additional information
-
not inhibited by deoxyrhamnojirimycin and 5-C-spirocyclopropyl-(5-demethyl-1-deoxy)-L-fuconojirimycin
-
additional information
-
chelating agents at a concentration of 10 mM do not affect the activity of Penicillium tardum alpha-L-rhamnosidase. No effect by 2-mercaptoethanol and EDTA at 10 mM
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
activates 70% at 10 mM. The effect of the Ca2+ cation may be related to the stabilization of the tertiary structure of the protein. Forming ionic bonds with two different amino acid residues, Ca2+ ions can act as a stabilizing bridge similar to disulfide bonds
EDTA
a slight activating influence on isoform RhaB1 is observed for EDTA at 10 mM
additional information
L-rhamnose induces the enzyme at transcriptional level, mechanism
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma, Bronchiolo-Alveolar
Interaction Analysis of Commercial Graphene Oxide Nanoparticles with Unicellular Systems and Biomolecules.
Carcinoma, Hepatocellular
Gynosaponin TN-1 producing from the enzymatic conversion of gypenoside XLVI by naringinase and its cytotoxicity on hepatoma cell lines.
Colitis
Anti-inflammatory activity of naringin and the biosynthesised naringenin by naringinase immobilized in microstructured materials in a model of DSS-induced colitis in mice
Neoplasms
Inhibitory effects of mulberry fruit extract in combination with naringinase on the allergic response in IgE-activated RBL-2H3 cells.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.138
4-nitrophenyl alpha-L-rhamnopyranoside
F6IEX3
pH 6.9, 37°C, mutant enzyme D763A
0.157
4-nitrophenyl alpha-L-rhamnopyranoside
F6IEX3
pH 6.9, 37°C, wild-type enzyme
0.159
4-nitrophenyl alpha-L-rhamnopyranoside
F6IEX3
pH 6.9, 37°C, mutant enzyme D552A
0.36
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, recombinant enzyme
0.457
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, mutant enzyme D594Q
0.458
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, mutant enzyme D594Q/G827K
0.46
4-nitrophenyl alpha-L-rhamnopyranoside
pH 7.5, 50°C, recombinant RhmA
0.476
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, wild-type enzyme
0.481
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, without additives
0.481
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, recombinant enzyme
0.493
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, in presence of 0.6 M sorbitol
0.5
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 10.5 (0.2M sodium phosphate buffer), 50°C
0.51
4-nitrophenyl alpha-L-rhamnopyranoside
isoform RhaB2
0.542
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, in presence of 1.0 M sorbitol
0.57
4-nitrophenyl alpha-L-rhamnopyranoside
isoform RhaB1
0.66
4-nitrophenyl alpha-L-rhamnopyranoside
pH 7.0, 50°C, recombinant RhmB
0.69
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, mutant enzyme Y316F
1.29 - 1.64
4-nitrophenyl alpha-L-rhamnopyranoside
recombinant wild-type enzyme, pH 7.0, 80°C
1.31
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, mutant enzyme W261Y
1.47
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, wild-type enzyme
1.47
4-nitrophenyl alpha-L-rhamnopyranoside
recombinant wild-type enzyme, pH 7.0, 80°C
1.6
4-nitrophenyl alpha-L-rhamnopyranoside
pH 7.0, 30°C, recombinant isozyme Ram1
1.9
4-nitrophenyl alpha-L-rhamnopyranoside
recombinant wild-type enzyme, pH 7.0, 80°C
1.94
4-nitrophenyl alpha-L-rhamnopyranoside
R4P072
recombinant wild-type enzyme, pH 7.0, 80°C
2.01
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, mutant enzyme Y302F
2.11
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, mutant enzyme R548A
3.12
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, mutant enzyme W555A
8.84
4-nitrophenyl alpha-L-rhamnopyranoside
pH 5.0, 60°C, mutant enzyme V529A
12.9
4-nitrophenyl alpha-L-rhamnopyranoside
pH 5.0, 60°C, wild-type enzyme
160.2
4-nitrophenyl alpha-L-rhamnopyranoside
F6IEX3
pH 6.9, temperature not specified in the publication
0.067
hesperidin
-
recombinant enzyme, pH 7.5, temperature not specified in the publication
0.59
naringin
-
recombinant enzyme, pH 7.5, temperature not specified in the publication
0.119
p-nitrophenyl-alpha-L-rhamnopyranoside
Q93RE8, Q93RE7
pH 7.0
0.282
p-nitrophenyl-alpha-L-rhamnopyranoside
Q93RE8, Q93RE7
pH 7.0
0.15
quercitrin
-
recombinant enzyme, pH 7.5, temperature not specified in the publication
0.031
rutin
-
recombinant enzyme, pH 7.5, temperature not specified in the publication
additional information
additional information
Q93RE7
2.5 micrograms per ml of purified protein used for the wild-type enzyme and 500 micrograms per ml for mutant enzymes
-
additional information
additional information
isozyme Ram2 does not follow a hyperbolic Michaelis-Menten correlation suggesting an oligomeric structure and an allosteric regulation. Ram2 displays sigmoidal responses to increasing substrate concentrations and exhibits positive substrate binding cooperativity
-
additional information
additional information
isozyme Ram2 does not follow a hyperbolic Michaelis-Menten correlation suggesting an oligomeric structure and an allosteric regulation. Ram2 displays sigmoidal responses to increasing substrate concentrations and exhibits positive substrate binding cooperativity
-
additional information
additional information
Michaelis?Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
the enzyme exhibited typical Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0246
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, mutant enzyme W261Y
0.0498
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, mutant enzyme Y316F
0.16
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, mutant enzyme W555A
0.55
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, mutant enzyme Y302F
1.77
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, mutant enzyme R548A
3.07
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, wild-type enzyme
6.85
4-nitrophenyl alpha-L-rhamnopyranoside
pH 7.0, 30°C, recombinant isozyme Ram1, calculated by BRENDA
14.3
4-nitrophenyl alpha-L-rhamnopyranoside
recombinant wild-type enzyme, pH 7.0, 80°C
15.6
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 10.5 (0.2M sodium phosphate buffer), 50°C
51.9
4-nitrophenyl alpha-L-rhamnopyranoside
recombinant wild-type enzyme, pH 7.0, 80°C
126
4-nitrophenyl alpha-L-rhamnopyranoside
F6IEX3
pH 6.9, 37°C, mutant enzyme D763A
146.8
4-nitrophenyl alpha-L-rhamnopyranoside
recombinant wild-type enzyme, pH 7.0, 80°C
217.8
4-nitrophenyl alpha-L-rhamnopyranoside
R4P072
recombinant wild-type enzyme, pH 7.0, 80°C
362.5
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, in presence of 1.0 M sorbitol
379.2
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, in presence of 0.6 M sorbitol
407.6
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, without additives
412
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, wild-type enzyme
434
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, mutant enzyme D594Q/G827K
458
4-nitrophenyl alpha-L-rhamnopyranoside
F6IEX3
pH 6.9, 37°C, mutant enzyme D552A
458
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, mutant enzyme D594Q
650
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, recombinant enzyme
692
4-nitrophenyl alpha-L-rhamnopyranoside
F6IEX3
pH 6.9, 37°C, wild-type enzyme
1065
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, recombinant enzyme
1743.29
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 55°C
5380
4-nitrophenyl alpha-L-rhamnopyranoside
pH 5.0, 60°C, mutant enzyme V529A
10200
4-nitrophenyl alpha-L-rhamnopyranoside
pH 5.0, 60°C, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
833.1
nairutin
-
recombinant wild-type enzyme, pH 5.0, 50°C, calculated by BRENDA
-
534.4
neohesperidin
-
recombinant wild-type enzyme, pH 5.0, 50°C, calculated by BRENDA
0.0188
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, mutant enzyme W261Y
0.0505
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, mutant enzyme W555A
0.0722
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, mutant enzyme Y316F
0.27
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, mutant enzyme Y302F
0.84
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, mutant enzyme R548A
2.09
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 6.5, 55°C, wild-type enzyme
4.28
4-nitrophenyl alpha-L-rhamnopyranoside
pH 7.0, 30°C, recombinant isozyme Ram1, calculated by BRENDA
31.2
4-nitrophenyl alpha-L-rhamnopyranoside
-
pH 10.5 (0.2M sodium phosphate buffer), 50°C
608.6
4-nitrophenyl alpha-L-rhamnopyranoside
pH 5.0, 60°C, mutant enzyme V529A
670
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, in presence of 1.0 M sorbitol
770
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, in presence of 0.6 M sorbitol
792
4-nitrophenyl alpha-L-rhamnopyranoside
pH 5.0, 60°C, wild-type enzyme
850
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, without additives
867
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, wild-type enzyme
900
4-nitrophenyl alpha-L-rhamnopyranoside
F6IEX3
pH 6.9, 37°C, mutant enzyme D763A
947
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, mutant enzyme D594Q/G827K
1001
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, mutant enzyme D594Q
1810
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, recombinant enzyme
2214
4-nitrophenyl alpha-L-rhamnopyranoside
pH 6.5, 65°C, recombinant enzyme
2900
4-nitrophenyl alpha-L-rhamnopyranoside
F6IEX3
pH 6.9, 37°C, mutant enzyme D552A
4400
4-nitrophenyl alpha-L-rhamnopyranoside
F6IEX3
pH 6.9, 37°C, wild-type enzyme
2610.5
hesperidin
-
recombinant wild-type enzyme, pH 5.0, 50°C, calculated by BRENDA
392.5
naringin
-
recombinant wild-type enzyme, pH 5.0, 50°C, calculated by BRENDA
364.2
rutin
-
recombinant wild-type enzyme, pH 5.0, 50°C, calculated by BRENDA
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0029
(2S,3R,4S)-benzyl-3,4-dihydroxy pyrrolidine
-
pH 6.7, 30°C, versus 4-nitrophenyl alpha-L-rhamnopyranoside
0.0026
(2S,3S,4R)-deacetyl anisomycin
-
pH 6.7, 30°C, versus 4-nitrophenyl alpha-L-rhamnopyranoside
0.058
(2S,3S,4S)-anisomycin
-
pH 6.7, 30°C, versus 4-nitrophenyl alpha-L-rhamnopyranoside
0.0029
(2S,3S,4S)-deacetyl anisomycin
-
pH 6.7, 30°C, versus 4-nitrophenyl alpha-L-rhamnopyranoside
0.0032
[4-([[(2S,3S,4R)-3,4-dihydroxypyrrolidin-2-yl]methyl]amino)-5-hydroxy-6-methylpyridin-2-yl]methyl dihydrogen phosphate
-
-
0.003
[4-([[(2S,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl]amino)-5-hydroxy-6-methylpyridin-2-yl]methyl dihydrogen phosphate
-
-
1.28
L-rhamnose
pH 7.5, 50°C, recombinant RhmA, versus 4-nitrophenyl alpha-L-rhamnopyranoside
1.4 - 6.5
L-rhamnose
recombinant wild-type enzyme, pH 7.0, 80°C
1.8
L-rhamnose
Q93RE7
crystallized complex with interacting site analyzed
2.5
L-rhamnose
-
pH 5.0, 37°C, versus 4-nitrophenyl alpha-L-rhamnopyranoside
2.56 - 4.94
L-rhamnose
recombinant wild-type enzyme, pH 7.0, 80°C
4.65
L-rhamnose
pH 7.0, 50°C, recombinant RhmB, versus 4-nitrophenyl alpha-L-rhamnopyranoside
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.3
L-rhamnose
Thermoclostridium stercorarium subsp. stercorarium
recombinant wild-type enzyme, pH 7.0, 80°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.57
1.2
-
purified recombinant wild-type enzyme, pH 5.0, 50°C, substrate rutin
1.4
-
purified recombinant wild-type enzyme, pH 5.0, 50°C, substrate naringin
11.5
purified recombinant enzyme, pH 6.0, 50°C, substrate 4-nitrophenyl beta-D-galactopyranoside
11.7
purified recombinant isozyme Ram2, pH 4.0, 50°C, substrate 4-nitrophenyl alpha-L-rhamnopyranoside
154.4
purified recombinant enzyme, pH 6.0, 50°C, substrate rutin
17.9
substrate 4-nitrophenyl alpha-L-rhamnopyranoside, pH 4.0, 40°C
2.13
purified recombinant enzyme, pH 7.0, 80°C, substrate 4-nitrophenyl alpha-L-rhamnopyranoside
2.2
-
purified recombinant wild-type enzyme, pH 5.0, 50°C, substrate neohesperidin
23.3
recombinant enzyme, pH and temperature not specified in the publication
29.89
-
purified enzyme, pH 7.0, 55°C, substrate 4-nitrophenyl-alpha-L-rhamnopyranoside
304.3
31.6
purified recombinant enzyme, pH 6.0, 50°C, substrate 4-nitrophenyl alpha-D-galactopyranoside
32.23
purified recombinant enzyme, pH 7.0, 80°C, substrate 4-nitrophenyl alpha-L-rhamnopyranoside
34.43
purified recombinant enzyme, pH 4.5, 60°C, substrate 4-nitrophenyl alpha-L-rhamnopyranoside
40.5
44.5
purified recombinant enzyme, pH 6.0, 50°C, substrate 4-nitrophenyl alpha-D-glucopyranoside
452
pH 6.5, 65°C, purified recombinant enzyme, substrate 4-nitrophenyl alpha-L-rhamnopyranoside
454
substrate: 4-nitrophenyl alpha-L-rhamnopyranoside, pH 6.5, 65°C, wild-type enzyme
486
substrate: 4-nitrophenyl alpha-L-rhamnopyranoside, pH 6.5, 65°C, mutant enzyme D594Q/G827K
49.3
-
recombinant enzyme, pH and temperature not specified in the publication
504
substrate: 4-nitrophenyl alpha-L-rhamnopyranoside, pH 6.5, 65°C, mutant enzyme D594Q
54.2
purified recombinant enzyme, pH 6.0, 50°C, substrate naringin
6.4
-
purified recombinant wild-type enzyme, pH 5.0, 50°C, substrate nairutin
64.7
7.38
purified recombinant enzyme, pH 7.0, 80°C, substrate 4-nitrophenyl alpha-L-rhamnopyranoside
711.9
activity of the recombinant overexpressed enzyme, pH and temperature not specified in the publication
8.2
purified recombinant enzyme, pH 6.0, 50°C, substrate 2-nitrophenyl alpha-D-glucopyranoside
8.5
-
purified recombinant wild-type enzyme, pH 5.0, 50°C, substrate hesperidin
87.9
purified recombinant enzyme, pH 6.0, 50°C, substrate hesperidin
additional information
0.57
recombinant enzyme, pH and temperature not specified in the publication
0.57
recombinant enzyme in optimized high-density production in Pichia pastoris, pH 5.0, 50°C
304.3
purified recombinant enzyme, pH 6.0, 50°C, substrate 4-nitrophenyl alpha-L-rhamnopyranoside
40.5
R4P072
purified recombinant enzyme, pH 7.0, 80°C, substrate 4-nitrophenyl alpha-L-rhamnopyranoside
40.5
R4P072
recombinant enzyme, pH and temperature not specified in the publication
64.7
purified recombinant isozyme Ram1, pH 5.5, 50°C, substrate 4-nitrophenyl-alpha-L-rhamnopyranoside
64.7
recombinant enzyme, pH and temperature not specified in the publication
additional information
the activities with hesperidin and naringin are 7240 U/ml and 945 U/ml, respectively, which are 10.63 times that of native alpha-L-rhamnosidase
additional information
Q93RE7
assay in a reaction system containing 0.4 mM p-nitrophenyl-alpha-L-rhamnopyranoside as a substrate and 50 mM potassium phosphate buffer, resultant p-nitrophenol concentration determined spectrophotometrically
additional information
Q93RE7
assayed in a reaction system containing 0.4 mM p-nitrophenyl-alpha-L-rhamnopyranoside as a substrate and 50 mM potassium phosphate buffer, resultant p-nitrophenol concentration determined spectrophotometrically
additional information
-
the isolate 005NJ retains 19% alpha-L-rhamnosidase activity at 7°C and 6% activity at 4°C, relative activity depends on carbon source, maximal specific activity obtained at concentrations of 0.5% (w/v) for L-rhamnose (967 U/mg) and apple pectin (382 U/mg)
additional information
-
activity analyzed at 4°C and 7°C, 100% activity arbitrarily established as the activity shown at 35°C, corresponds to 151 U/ml in Ralstonia pickettii, activity about 5% at 4°C and about 15% at 7°C determined
additional information
activity measured under different conditions of pH and temperature, free cells and immobilized cells compared to defined conditions of large scale production of rhamnose, assay described, full degradation of 7.9 mM naringin by running the reactor at 1 ml per min at 50°C, optimal flow rates estimated, after four days substrate degradation capacity decreased by 10 to 15%
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
4.5
4.5 - 5
4.5 - 5.5
5.5
5.5 - 6.5
6.5
6.5 - 7
7.5
7.8
6.5
wild-type enzyme, mutant enzyme D594Q and mutant enzyme G827K/D594Q
7.8
optimal pH of enzyme activity using cells immobilized in alginate beads
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 10
-
40% of maximal activity at pH 4.0, 10% at pH 10.0
2 - 5
3 - 8
3.5 - 5.5
-
at pH ranging from 3.5 to 5.5 still the enzyme maintains more than 60% of the optimal pH activity
4 - 7
over 70% of maximal activity within this range, profile overview
4 - 8
when the enzyme is in the condition of pH 4.0 to 5.0 or pH 7.0 to 8.0, its activity decreases dramatically to 40% yield or even less, soluble enzyme
4.4 - 5.5
isoform RhaB2 maintains over 60% of its activity in the pH range from 4.4 to 5.5
4.5 - 8
5 - 6.3
over 90% of maximal activity within this range, recombinant enzyme
5 - 7.5
5.5 - 6.6
R4P072
over 90% of maximal activity within this range, recombinant enzyme
5.5 - 8.6
pH 5.5: about 80% of maximal activity, high activity (more than 60%) at alkaline pH 7.5-8.6
5.5 - 9.5
activity measured, no enzyme activity at pH 4.3 of cells on beads in contrast to measured activity of free cells
5.6 - 6.3
over 90% of maximal activity within this range, recombinant enzyme
6 - 7.5
-
over 70% of maximal activity within this range, profile overview
7.9 - 8.8
F6IEX3
the enzyme retains 47% and 36% of activity at pH 7.9 and 8.8
3 - 8
-
pH 3.0: about 60% of maximal activity, pH 8.0: about 50% of maximal activity
3 - 8
highest activity at pH 3.0, 50% of maximal activity at pH 6.0, 40% at pH 8.0
4.5 - 8
over 40% of maximal activity within this range, profile overview
5 - 7.5
wild-type enzyme and mutant enzymes D594Q and G827K/D594Q retain more than 90% relative activity over the pH range 5.0-7.5
5 - 7.5
isoform RhaB1 maintains over 60% of its activity in the pH range from 5.0 to 7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
40
45
50
55
55 - 60
60
65
70
40
-
estimated by activity assay, 6% activity retained at 4°C, half-life of 4 min at 50°C indicates thermo-sensitivity
50
optimal temperature for the flow rate of the developed bioreactor over a time of three days, optimal temperature for stability of cells immobilized on beads, full degradation of naringin measured
55
hydrolysis of epimedin C, hydrolysis of 4-nitrophenyl alpha-L-rhamnopyranoside
60
recombinant enzyme with substrate rutin
60
alginate immobilized cells and free cells, optimal running temperature of the developed bioreactor over a time of 60 min
65
wild-type enzyme, mutant enzyme D594Q and mutant enzyme G827K/D594Q
65
recombinant enzyme with substrate 4-nitrophenyl alpha-L-rhamnopyranoside
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 75
activity range, profile overview. 10% of maximal activity at 10°C and 75°C, 50% at 45°C and 70°C, maximal activity at 60°C
20 - 60
highest activity at 60°C, 80% of maximal activity at 40°C, 25% at 20°C
20 - 70
over 70% of maximal activity within this range, profile overview
30 - 60
30 - 70
32 - 45
F6IEX3
32°C: about 55% of maximal activity, 45°C: about 65% of maximal activity
35 - 65
35°C: about 50% of maximal activity, 65°C: about 70% of maximal activity
35 - 70
-
over 40% of maximal activity within this range, profile overview
36 - 63
over 80% of maxximal activity within this range, recombinant enzyme
37 - 90
hydrolysis of 4-nitrophenyl-alpha-L-rhamnopyranoside at 37°C is catalyzed at 17% of the activity compared to that at 90°C
4 - 40
-
activity measured, 6% activity maintained at 4°C, thermo-inactivation above 50°C
40 - 60
40 - 70
-
40°C: about 55% of maximal activity, 70°C: about 30% of maximal activity
45 - 75
50 - 60
50 - 70
62 - 76
over 80% of maximal activity within this range, recombinant enzyme
65 - 75
65°C: temperature-optimum of wild-type enzyme and mutant enzymes D594Q and G827K/D594Q. At 70 °C, the wild type enzyme retains 88.4% of its maximum activity, whereas the D594Q and G827K/D594Q mutant enzymes retain 96.6% and 98.5% of their maximum activities, respectively. At 75°C, the wild-type enzyme retains 48.5% of its maximum activity, whereas the D594Q and G827K/D594Q mutant enzymes retain 71.2% and 81.1% of their maximum activities, respectively
74 - 91
over 80% of maximal activity within this range, recombinant enzyme
76.5 - 93
R4P072
over 80% of maximal activity within this range, recombinant enzyme
30 - 60
the enzyme shows relative activities over 64% from 30 to 60°C
30 - 70
30°C: about 65% of maximal activity, 70°C: about 55% of maximal activity
30 - 70
over 40% of maximal activity within this range, profile overview
40 - 60
40°C: about 50% of maximal activity, 60°C: about 80% of maximal activity, hydrolysis of 4-nitrophenyl alpha-L-rhamnopyranoside
45 - 75
-
45°C: about 60% of maximal activity, 75°C: about 45% of maximal activity
45 - 75
-
activity is more than 50% of the maximum activity in the temperature range 45°C-75°C
50 - 60
50°C: about 65% of maximal activity, 60°C: about 75% of maximal activity, hydrolysis of epimedin C
50 - 70
55°C: about 50% of maximal activity, 70°C: about 40% of maximal activity, immobilized enzyme
50 - 70
isoform RhaB2 is most active at temperatures between 50 and 70°C, still showing 70% relative activity at 70°C
50 - 70
activity measured, flow rates of bioreactor determined
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6
additional information
additional information
shows microheterogenity upon isoelectric focusing
additional information
shows microheterogenity upon isoelectric focusing
additional information
-
shows microheterogenity upon isoelectric focusing
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 90, FFDCL-90, and strain 39, FFDCL-39, isolated from traditional Chinese Koji
-
-
brenda
Aspergillus niger CCTCC M 2018240
formerly Anaerocellum thermophilum, isolated from a thermal spring in Kamchatka, Russia
UniProt
brenda
formerly Anaerocellum thermophilum, isolated from a thermal spring in Kamchatka, Russia
UniProt
brenda
formerly Anaerocellum thermophilum, isolated from a thermal spring in Kamchatka, Russia
UniProt
brenda
formerly Anaerocellum thermophilum, isolated from a thermal spring in Kamchatka, Russia
UniProt
brenda
formerly Anaerocellum thermophilum, isolated from a thermal spring in Kamchatka, Russia
UniProt
brenda
Lactiplantibacillus plantarum ATCC BAA-793
Lactiplantibacillus plantarum NCIMB 8826
formerly Clostridium stercorarium, isolated from a compost heap
UniProt
brenda
formerly Clostridium stercorarium, isolated from a compost heap
UniProt
brenda
synthesized by only a few members of the Aspergillus flavus group
-
-
brenda
ene rhaB, when grown on gellan medium, only this isoform is expressed
Q93RE7
SwissProt
brenda
ene rhaB, when grown on gellan medium, only this isoform is expressed
Q93RE7
SwissProt
brenda
naringinase: complex of beta-D-glucosidase and alpha-L-rhamnosidase
-
-
brenda
i.e. Pseudomonas paucimobilis, strain FP2001, JCM 10661, gene rhaM
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
recombinant Echerichia coli cells carrying the rhmA gene of Thermomicrobia bacterium
brenda
-
culture condition: L-rhamnose as sole carbon source, enzyme biosynthesis is repressed by glucose
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
the enzyme contains no signal sequence peptide
-
brenda
additional information
-
the enzyme contains no signal sequence peptide
-
-
brenda
additional information
-
the enzyme contains no signal sequence peptide
-
-
brenda
additional information
-
the enzyme contains no signal sequence peptide
-
-
brenda
additional information
-
the enzyme contains no signal sequence peptide
-
-
brenda
additional information
the enzyme contains no signal sequence peptide
-
brenda
additional information
-
the enzyme contains no signal sequence peptide
-
-
brenda
additional information
R4P072
the enzyme contains no signal sequence peptide
-
brenda
additional information
-
the enzyme contains no signal sequence peptide
-
-
brenda
additional information
-
the enzyme contains no signal sequence peptide
-
-
brenda
additional information
-
the enzyme contains no signal sequence peptide
-
-
brenda
additional information
-
the enzyme contains no signal sequence peptide
-
-
brenda
additional information
the enzyme contains no signal sequence peptide
-
brenda
additional information
-
the enzyme contains no signal sequence peptide
-
-
brenda
additional information
-
the enzyme contains no signal sequence peptide
-
-
brenda
additional information
-
the enzyme contains no signal sequence peptide
-
-
brenda
additional information
-
the enzyme contains no signal sequence peptide
-
-
brenda
additional information
-
the enzyme contains no signal sequence peptide
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
the enzyme belongs to the glycoside hydrolase family 78, GH78
evolution
the enzyme belongs to the glycoside hydrolase family 78, GH78
evolution
R4P072
the enzyme belongs to the glycoside hydrolase family 106, GH106
evolution
the enzyme belongs to the glycoside hydrolase family 106, GH106
evolution
the enzyme belongs to the glycoside hydrolase family 106, GH106
evolution
the enzyme belongs to the glycoside hydrolase family 78, GH78
evolution
the enzyme belongs to the glycoside hydrolase family 106, GH106
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
Q93RE8, Q93RE7
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
F6IEX3
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
R4P072
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
three-dimensional structure simulation indicates that the enzyme belongs to the glycoside hydrolase family 78, GH78
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
evolution
-
the enzyme belongs to the glycoside hydrolase family 106, GH106
evolution
the enzyme belongs to the glycoside hydrolase family 78, GH78
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 78, GH78
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 78, GH78
-
evolution
Lactiplantibacillus plantarum NCIMB 8826
-
the enzyme belongs to the glycoside hydrolase family 78, GH78
-
evolution
Lactiplantibacillus plantarum NCIMB 8826
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
Lactiplantibacillus plantarum ATCC BAA-793
-
the enzyme belongs to the glycoside hydrolase family 78, GH78
-
evolution
Lactiplantibacillus plantarum ATCC BAA-793
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 106, GH106
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 106, GH106
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 106, GH106
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 106, GH106
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 106, GH106
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
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evolution
Aspergillus niger JMU-TS528
-
the enzyme belongs to the glycoside hydrolase family 78, GH78
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evolution
Aspergillus niger JMU-TS528
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 106, GH106
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 78, GH78
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 78, GH78
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 106, GH106
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 106, GH106
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 106, GH106
-
evolution
Bacteroides thetaiotaomicron JCM 5827
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
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evolution
Bacteroides thetaiotaomicron CCUG 10774
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 106, GH106
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 106, GH106
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 106, GH106
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 106, GH106
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 106, GH106
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
Klebsiella oxytoca BUCSAV 143
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
Klebsiella oxytoca CCM 1901
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
Aspergillus niger CCTCC M 2018240
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
Aspergillus niger CCTCC M 2018240
-
three-dimensional structure simulation indicates that the enzyme belongs to the glycoside hydrolase family 78, GH78
-
evolution
Aspergillus terreus CCF3059
-
the enzyme belongs to the glycoside hydrolase family 78, GH78
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
evolution
Talaromyces stollii CLY-6
-
based on amino acid sequence similarity, alpha-L-rhamnosidases of microbial origin can be classified into GH13, GH78 and GH106 glycoside hydrolase families in the CAZy database. The analysis of the protein structure and reaction mechanism of different alpha-L-rhamnosidase species revealed that they have some differences: GH78 family alpha-L-rhamnosidase contains five structural domains and reacts through the substrate binding to the catalytic domain of the barrel structure of (alpha/alpha)6, GH106 family lpha-L-rhamnosidase has a (beta/alpha)8-barrel structure containing five structural domains, and GH13 family alpha-L-rhamnosidase crystal structure has not yet been resolved, and its properties are highly similar to the sequence of amylase but cannot hydrolyze soluble starch
-
physiological function
isozymes Ram1 and Ram2 from Lactobacillus plantarum strain WCFS1 belong to the GH78 alpha-L-rhamnosidases family that catalyzes the hydrolysis of alpha-L-rhamnosyl-linkages through an acid-base catalyzed single displacement (inverting) mechanism. Isozymes Ram1 and Ram2 are quite different in functionality
physiological function
isozymes Ram1 and Ram2 from Lactobacillus plantarum strain WCFS1 belong to the GH78 alpha-L-rhamnosidases family that catalyzes the hydrolysis of alpha-L-rhamnosyl-linkages through an acid-base catalyzed single displacement (inverting) mechanism. Allosteric regulation, exhibiting positive substrate binding cooperativity, a mechanism that implies an oligomeric quaternary structure. Isozymes Ram1 and Ram2 are quite different in functionality
physiological function
-
alpha-L-rhamnosidase can release the terminal L-rhamnose from a series of glycosides, glycolipids, and some natural products by cleaving alpha-1,2, alpha-1,3, alpha-1,4, or alpha-1,6 glycosidic bonds
physiological function
alpha-L-rhamnosidase catalyzes hydrolysis of the terminal alpha-L-rhamnose from various natural rhamnoglycosides, including naringin and hesperidin
physiological function
-
alpha-L-rhamnosidases cleave terminal alpha-L-rhamnose from natural glycosides, including flavonoid glycosides. alpha-L-Rhamnosidases play a role in enhancing the aroma of grape juices and derived beverages
physiological function
R4P072
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
physiological function
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
physiological function
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
physiological function
alpha-L-rhamnosidase is a hydrolase that specifically releases terminal L-rhamnose groups from various natural glycoside compounds
physiological function
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
physiological function
the enzyme from Aspergillus niger strain CCTCC M 2018240 is a secreted naringinase
physiological function
alpha-L-rhamnosidase from Alternaria sp. L1, RhaL1 can perform one-step rhamnosylation of anticancer drugs, including 2'-deoxy-5-fluorouridine (FUDR), cytosine arabinoside (Ara C), and hydroxyurea (Hydrea). The rhamnosylated drugs exhibit little cytotoxic effects on cancer cells, but efficiently restore cytotoxic activity when incubated with exogenous alpha-L-rhamnosidase. The fluorescence probe Rha-RhB displays much higher cell affinity and cellular internalization rate of oral cancer cell KB and breast cancer cell MDA-MB-231 than that of the normal epithelial cells MCF 10A, suggesting that the rhamnose moiety can mediate the specific internalization of rhamnosylated compounds into cancer cells, which greatly facilitated their applications for cancer-targeting drug delivery
physiological function
-
the enzyme can convert flavonoids of epimedium, it converts epoetin C to produce icariin. Only icariin is currently included in the Chinese Pharmacopoeia as a quality marker (Q-marker) for epimedium flavonoids. Icariin has the functions of anti-aging, anti-inflammation, antioxidation, anti-osteoporosis, and ameliorating fibrosis
physiological function
-
the enzyme can convert flavonoids of epimedium, it converts epoetin C to produce icariin. Only icariin is currently included in the Chinese Pharmacopoeia as a quality marker (Q-marker) for epimedium flavonoids. Icariin has the functions of anti-aging, anti-inflammation, antioxidation, anti-osteoporosis, and ameliorating fibrosis
-
physiological function
-
alpha-L-rhamnosidase catalyzes hydrolysis of the terminal alpha-L-rhamnose from various natural rhamnoglycosides, including naringin and hesperidin
-
physiological function
-
alpha-L-rhamnosidase catalyzes hydrolysis of the terminal alpha-L-rhamnose from various natural rhamnoglycosides, including naringin and hesperidin
-
physiological function
Lactiplantibacillus plantarum NCIMB 8826
-
isozymes Ram1 and Ram2 from Lactobacillus plantarum strain WCFS1 belong to the GH78 alpha-L-rhamnosidases family that catalyzes the hydrolysis of alpha-L-rhamnosyl-linkages through an acid-base catalyzed single displacement (inverting) mechanism. Isozymes Ram1 and Ram2 are quite different in functionality
-
physiological function
Lactiplantibacillus plantarum NCIMB 8826
-
isozymes Ram1 and Ram2 from Lactobacillus plantarum strain WCFS1 belong to the GH78 alpha-L-rhamnosidases family that catalyzes the hydrolysis of alpha-L-rhamnosyl-linkages through an acid-base catalyzed single displacement (inverting) mechanism. Allosteric regulation, exhibiting positive substrate binding cooperativity, a mechanism that implies an oligomeric quaternary structure. Isozymes Ram1 and Ram2 are quite different in functionality
-
physiological function
Lactiplantibacillus plantarum ATCC BAA-793
-
isozymes Ram1 and Ram2 from Lactobacillus plantarum strain WCFS1 belong to the GH78 alpha-L-rhamnosidases family that catalyzes the hydrolysis of alpha-L-rhamnosyl-linkages through an acid-base catalyzed single displacement (inverting) mechanism. Isozymes Ram1 and Ram2 are quite different in functionality
-
physiological function
Lactiplantibacillus plantarum ATCC BAA-793
-
isozymes Ram1 and Ram2 from Lactobacillus plantarum strain WCFS1 belong to the GH78 alpha-L-rhamnosidases family that catalyzes the hydrolysis of alpha-L-rhamnosyl-linkages through an acid-base catalyzed single displacement (inverting) mechanism. Allosteric regulation, exhibiting positive substrate binding cooperativity, a mechanism that implies an oligomeric quaternary structure. Isozymes Ram1 and Ram2 are quite different in functionality
-
physiological function
-
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
-
physiological function
-
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
-
physiological function
-
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
-
physiological function
-
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
-
physiological function
-
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
-
physiological function
Aspergillus niger JMU-TS528
-
alpha-L-rhamnosidase is a hydrolase that specifically releases terminal L-rhamnose groups from various natural glycoside compounds
-
physiological function
-
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
-
physiological function
-
alpha-L-rhamnosidase catalyzes hydrolysis of the terminal alpha-L-rhamnose from various natural rhamnoglycosides, including naringin and hesperidin
-
physiological function
-
alpha-L-rhamnosidase catalyzes hydrolysis of the terminal alpha-L-rhamnose from various natural rhamnoglycosides, including naringin and hesperidin
-
physiological function
-
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
-
physiological function
-
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
-
physiological function
-
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
-
physiological function
-
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
-
physiological function
-
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
-
physiological function
-
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
-
physiological function
-
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
-
physiological function
-
alpha-L-rhamnosidases are enzymes that catalyse the hydrolysis of alpha-L-rhamnosyl-linkages in compounds containing terminal alpha-L-rhamnose. The alpha-L-rhamnosidase removes the terminal L-rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside
-
physiological function
Aspergillus niger CCTCC M 2018240
-
the enzyme from Aspergillus niger strain CCTCC M 2018240 is a secreted naringinase
-
physiological function
Papiliotrema laurentii ZJU-L07
-
alpha-L-rhamnosidase can release the terminal L-rhamnose from a series of glycosides, glycolipids, and some natural products by cleaving alpha-1,2, alpha-1,3, alpha-1,4, or alpha-1,6 glycosidic bonds
-
additional information
structure-function analysis of wild-type and mutant enzymes, detailed overview
additional information
-
the catalytic residues of AoRhaA are suggested to be Asp254 and Glu524, and their catalytic roles are confirmed by mutational studies of D254N and E524Q variants, which lose their activity completely
additional information
R4P072
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
additional information
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
additional information
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
additional information
quantum chemistry calculations show that charge difference of the C-O atoms of the alpha-1,2, alpha-1,3 and alpha-1,6 bonds indicate that alpha-1,6 bond is most easily broken and alpha-1,3 bond is the most stable. Molecular dynamics simulations reveal that the key residue Trp359 may affect substrate specificity. The main catalytic sites of N12-Rha are located in the (alpha/alpha)6-barrel domain. Molecular docking of protein-ligand binding, followed by molecular dynamics simulation of the complexes of alpha-L-rhamnosidase and different substrates, analysis of the substrate structure-specificity relationship
additional information
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
additional information
-
the modelled enzyme structure shows highly conserved rhamnose- and calcium-binding residues in a shallow active site that is housed in the (beta/alpha)8 domain. Analysis of the electrostatic potentials and amino acid composition of the substrate binding pocket offering insight into the substrate preference of RHA-P for glycosylated aryl compounds such as hesperidin, naringin, rutin, and quercitrin, over polysaccharides, in silico docking, overview. Structure comparison with enzyme BT0986 (PDB ID 5MQN) from Bacteroides thetaiotaomicron. The catalytic residue in enzyme RHA-P is E506. The structure of BT0986 with bound substrate is also used as a template to model rhamnose into the RHA-P active site
additional information
-
structure-function analysis of wild-type and mutant enzymes, detailed overview
-
additional information
-
structure-function analysis of wild-type and mutant enzymes, detailed overview
-
additional information
-
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
-
additional information
-
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
-
additional information
-
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
-
additional information
-
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
-
additional information
-
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
-
additional information
Aspergillus niger JMU-TS528
-
quantum chemistry calculations show that charge difference of the C-O atoms of the alpha-1,2, alpha-1,3 and alpha-1,6 bonds indicate that alpha-1,6 bond is most easily broken and alpha-1,3 bond is the most stable. Molecular dynamics simulations reveal that the key residue Trp359 may affect substrate specificity. The main catalytic sites of N12-Rha are located in the (alpha/alpha)6-barrel domain. Molecular docking of protein-ligand binding, followed by molecular dynamics simulation of the complexes of alpha-L-rhamnosidase and different substrates, analysis of the substrate structure-specificity relationship
-
additional information
-
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
-
additional information
-
structure-function analysis of wild-type and mutant enzymes, detailed overview
-
additional information
-
structure-function analysis of wild-type and mutant enzymes, detailed overview
-
additional information
-
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
-
additional information
-
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
-
additional information
-
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
-
additional information
-
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
-
additional information
-
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
-
additional information
-
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
-
additional information
-
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
-
additional information
-
GH106/GH78 enzyme structure homology study, neighbour-joining tree based on a structural alignment with amino acid sequence of rhamnosidases
-
Show AA Sequence and Transmembrane Helices (9668 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
105000
Q93RE8, Q93RE7
1 * 106000, deduced from gene sequence, 1 * 105000, SDS-PAGE
106000
85000
90000
95000
98000
98300
Q93RE8, Q93RE7
5 * 98300, deduced from gene sequence, 5 * 98000, SDS-PAGE
106000
Q93RE8, Q93RE7
1 * 106000, deduced from gene sequence, 1 * 105000, SDS-PAGE
98000
Q93RE8, Q93RE7
5 * 98300, deduced from gene sequence, 5 * 98000, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
monomer or dimer
oligomer
pentamer
tetramer
additional information
?
x * 71200, about, sequence calculation, x * 70000, recombinant His-tagged enzyme, SDS-PAGE
?
Aspergillus niger ATCC MYA-4892
-
x * 71200, about, sequence calculation, x * 70000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 71200, about, sequence calculation, x * 70000, recombinant His-tagged enzyme, SDS-PAGE
-
?
Aspergillus niger FGSC A1513
-
x * 71200, about, sequence calculation, x * 70000, recombinant His-tagged enzyme, SDS-PAGE
-
?
x * 96900, about, sequence calculation, x * 130000, recombinant enzyme, SDS-PAGE
?
Aspergillus terreus CCF3059
-
x * 96900, about, sequence calculation, x * 130000, recombinant enzyme, SDS-PAGE
-
?
-
x * 115900, recombinant His6-tagged enzyme, SDS-PAGE
-
?
x * 121300, recombinant His6-tagged enzyme, SDS-PAGE
?
-
x * 121300, recombinant His6-tagged enzyme, SDS-PAGE
-
homodimer
Q93RE7
crystallized form, 1908 amino acids of residues 3-956, 43 glycerol molecules, four calcium ions, 1755 water molecules identified in the crystallized form
homodimer
-
crystallized form, 1908 amino acids of residues 3-956, 43 glycerol molecules, four calcium ions, 1755 water molecules identified in the crystallized form
-
monomer
Q93RE8, Q93RE7
1 * 106000, deduced from gene sequence, 1 * 105000, SDS-PAGE
monomer
-
1 * 106000, deduced from gene sequence, 1 * 105000, SDS-PAGE
-
monomer or dimer
R4P072
x * 116600, recombinant His6-tagged enzyme, SDS-PAGE
monomer or dimer
-
x * 116600, recombinant His6-tagged enzyme, SDS-PAGE
-
monomer or dimer
-
x * 116600, recombinant His6-tagged enzyme, SDS-PAGE
-
monomer or dimer
-
x * 116600, recombinant His6-tagged enzyme, SDS-PAGE
-
monomer or dimer
-
x * 116600, recombinant His6-tagged enzyme, SDS-PAGE
-
pentamer
Q93RE8, Q93RE7
5 * 98300, deduced from gene sequence, 5 * 98000, SDS-PAGE
pentamer
-
5 * 98300, deduced from gene sequence, 5 * 98000, SDS-PAGE
-
additional information
-
the catalytic domain is represented by an (alpha/alpha)6-barrel with the active site located in a deep cleft, and two beta-sheet domains are also present in the N- and C-terminal sites of the catalytic domain, crystal structure analysis
additional information
the structure of alpha-L-rhamnosidase consists of one alpha-domain (domain A) and four beta-domains (domains N, E, F and C). Domain A, which has an (alpha/alpha)6-barrel structure, is the catalytic module, while domains N, E, F and C consist almost solely of beta-strands and surround the catalytic module
additional information
-
the structure of alpha-L-rhamnosidase consists of one alpha-domain (domain A) and four beta-domains (domains N, E, F and C). Domain A, which has an (alpha/alpha)6-barrel structure, is the catalytic module, while domains N, E, F and C consist almost solely of beta-strands and surround the catalytic module
-
additional information
-
the structure of alpha-L-rhamnosidase consists of one alpha-domain (domain A) and four beta-domains (domains N, E, F and C). Domain A, which has an (alpha/alpha)6-barrel structure, is the catalytic module, while domains N, E, F and C consist almost solely of beta-strands and surround the catalytic module
-
additional information
-
the structure of alpha-L-rhamnosidase consists of one alpha-domain (domain A) and four beta-domains (domains N, E, F and C). Domain A, which has an (alpha/alpha)6-barrel structure, is the catalytic module, while domains N, E, F and C consist almost solely of beta-strands and surround the catalytic module
-
additional information
-
the structure of alpha-L-rhamnosidase consists of one alpha-domain (domain A) and four beta-domains (domains N, E, F and C). Domain A, which has an (alpha/alpha)6-barrel structure, is the catalytic module, while domains N, E, F and C consist almost solely of beta-strands and surround the catalytic module
-
additional information
the enzyme possesses a highly conserved C-terminal region
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
only N-glycosylation, about 24% carbohydrate
glycoprotein
only N-glycosylation, about 15% carbohydrate
glycoprotein
degree of N-glycosylation about 22%, sequence contains 13 putative N-glycosylation sites
glycoprotein
-
five asparagine attached N-acetylglucosamine molecules are observed. Sugar chain cleavage by endo-beta-N-acetylglucosaminidase H
glycoprotein
the enzyme is secreted in the glycosylated form, which contains approximately 14 kDa of glycosidic chain
glycoprotein
Aspergillus tubingensis JMU-TS529
-
the enzyme is secreted in the glycosylated form, which contains approximately 14 kDa of glycosidic chain
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified deglycosylated wild-type enzyme, hanging drop vapor diffusion method, 9 mg/ml protein solution is mixed with crystallization solution conatining 0.2 M ammonium acetate, 0.1 M Bis-Tris, pH 5.5, and 23% PEG 3350, X-ray diffraction structure determination and analysis at 2.51 A resolution, molecular replacement and modelling
-
X-ray structure of the GH78 family alpha-L-rhamnosidase from Aspergillus terreus has been determined at 1.38 A resolution using the sulfur single-wavelength anomalous dispersion phasing method
native and selenomethionine-derivaties, 1.9 A resolution with a final R-factor of 18.2%, hanging-drop method, data-collection and statistics indicated, overall structure shown, quaternary structure, catalytic domain and active cleft determined, complex with the reaction product rhamnose determined and refined at 2.1 A with a final R-factor of 19.5%
Q93RE7
native and selenomethionine-derivaties, crystallized at 293 K, hanging-drop vapour diffusion with PEG 8000 as a precipitant, data collection and statistics indicated
Q93RE7
hanging drop vapor diffusion method, crystal structure is determined at 2.7 A resolution with rhamnose bound in the active site of the catalytic domain. The homodimeric structure is significantly smaller than those of the other previously determined GH78 structures. Nevertheless, the enzyme displays alpha-rhamnosidase activity when assayed in vitro, suggesting that the additional structural domains found in the related enzymes are dispensible for function
purified recombinant His-tagged enzyme, hanging drop vapor diffusion method, mixing of 0.002 ml of 7 mg/ml protein solution with 0.001 ml of a precipitant solution containing 0.1M MES, pH 6.8, 6-7% Tascimate pH 5.0, 2-10mM Tris, pH 7.5, 10% w/w PEG 20000, 6-10% glycerol, and 0.01% NaN3, and 0.001 ml of RHA-P microseeds in precipitant solution, 2 weeks, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
W261Y
-
mutant enzyme with improved product yield in synthesis of rhamnose-containing chemicals through reverse hydrolysis reaction with rhamnose as glycosyl donor. Reverse hydrolysis is accelerated with 43.7% in relative yield compared to the wild-type enzyme. Based on 3D structural modeling, it is supposed that the improved yield of mutant W261Y is due to the adjustment of the spatial position of the putative catalytic acid residue Asp257. Mutant W261Y also exhibits a shift in the pH-activity profile in hydrolysis reaction, indicating that introducing of a polar residue in the active site cavity may affect the catalysis behavior of the enzyme
Y302F
-
mutant enzyme with improved product yield in synthesis of rhamnose-containing chemicals through reverse hydrolysis reaction with rhamnose as glycosyl donor. Reverse hydrolysis is accelerated with 33.3% in relative yield compared to the wild-type enzyme
Y316F
-
mutant enzyme with improved product yield in synthesis of rhamnose-containing chemicals through reverse hydrolysis reaction with rhamnose as glycosyl donor. Reverse hydrolysis is accelerated with 19.8% in relative yield compared to the wild-type enzyme
K406R/K573R
to improve the thermostability of the enzyme multiple arginine residues are introduced into the r-Rha1 sequence to replace several lysine residues that located on the surface of the folded enzyme. Hinted by in silico analysis, five surface Lys residues (K134, K228, K406, K440, K573) are targeted to produce a list of 5 single-residue mutants and 4 multiple-residue mutants using site-directed mutagenesis. Among these mutants, K406R/K573R shows the best thermostability improvement. The half-life of this mutant's enzyme activity increased 3 h at 60°C, 23 min at 65°C, and 3.5 min at 70°C, when compared with the wild type. With the enhanced thermostability, the mutant enzyme, K406R/K573R, has potentially broadened the applications of alpha-L-rhamnosidase in food processing industry
V529A
mutant enzyme with improved thermostability, improved substrate affinity and better resistance to the inhibition of glucose
K406R/K573R
Aspergillus niger JMU-TS528
-
to improve the thermostability of the enzyme multiple arginine residues are introduced into the r-Rha1 sequence to replace several lysine residues that located on the surface of the folded enzyme. Hinted by in silico analysis, five surface Lys residues (K134, K228, K406, K440, K573) are targeted to produce a list of 5 single-residue mutants and 4 multiple-residue mutants using site-directed mutagenesis. Among these mutants, K406R/K573R shows the best thermostability improvement. The half-life of this mutant's enzyme activity increased 3 h at 60°C, 23 min at 65°C, and 3.5 min at 70°C, when compared with the wild type. With the enhanced thermostability, the mutant enzyme, K406R/K573R, has potentially broadened the applications of alpha-L-rhamnosidase in food processing industry
-
V529A
Aspergillus niger JMU-TS528
-
mutant enzyme with improved thermostability, improved substrate affinity and better resistance to the inhibition of glucose
-
D117N
-
site-directed mutagenesis, the mutant shows moderately reduced activity
D249N
-
site-directed mutagenesis, the mutant shows highly reduced activity
D254N
-
site-directed mutagenesis of the catalytic residue, inactive mutant
D261N
-
site-directed mutagenesis, the mutant shows highly reduced activity
E524Q
-
site-directed mutagenesis of the catalytic residue, inactive mutant
D594Q
half-life at 70°C is prolonged by 2.1fold. Analysis of the 3D structure shows that in the thermostable variants the number of hydrogen bonds and salt bridges is increased, explaining the enhanced thermostability. The KM value for 4-nitrophenyl-alpha-L-rhamnopyranoside decreases by 4.0%. The kcat/KM value increases by 15.5%. The mutant enzyme exhibits markedly improved isoquercitrin yield at 70°C that increases by 13.5%
D594Q/G827K
half-life at 70°C is prolonged by 2.3fold. Analysis of the 3D structure shows that in the thermostable variants the number of hydrogen bonds and salt bridges is increased, explaining the enhanced thermostability. The KM value for 4-nitrophenyl-alpha-L-rhamnopyranoside decreases by 3.8%. The kcat/KM value increases by 9.2%. The mutant enzyme exhibits markedly improved isoquercitrin yield at 70°C that increases by 11.0%
D567N
Q93RE7
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
D579N
Q93RE7
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
E572Q
Q93RE7
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
E841Q
Q93RE7
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
D567N
-
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
-
D579N
-
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
-
E572Q
-
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
-
E841Q
-
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
-
D330A
2350fold reduction in specific activity as compared to the wild-type enzyme
D335A
560fold reduction in specific activity as compared to the wild-type enzyme
D335E
2770fold reduction in specific activity as compared to the wild-type enzyme
D335N
1170fold reduction in specific activity as compared to the wild-type enzyme
D342A
7670fold reduction in specific activity as compared to the wild-type enzyme
E595A
6970fold reduction in specific activity as compared to the wild-type enzyme
E595Q
19170fold reduction in specific activity as compared to the wild-type enzyme
H620A
40fold reduction in specific activity as compared to the wild-type enzyme
R334A
280fold reduction in specific activity as compared to the wild-type enzyme
W339A
1230fold reduction in specific activity as compared to the wild-type enzyme
W440A
530fold reduction in specific activity as compared to the wild-type enzyme
Y383A
740fold reduction in specific activity as compared to the wild-type enzyme
D335A
-
560fold reduction in specific activity as compared to the wild-type enzyme
-
D335E
-
2770fold reduction in specific activity as compared to the wild-type enzyme
-
D335N
-
1170fold reduction in specific activity as compared to the wild-type enzyme
-
E595A
-
6970fold reduction in specific activity as compared to the wild-type enzyme
-
E595Q
-
19170fold reduction in specific activity as compared to the wild-type enzyme
-
D552A
D763A
additional information
D552A
F6IEX3
kcat/KM value is 65% of the wild-type value. This reduced catalytic efficiency is mainly due to a significative variation in the turnover number, defined by the kcat value, for which a 34% decrease is observed
D763A
F6IEX3
kcat/KM value is 21% of the wild-type value. A 82% decrease in kcat is retrieved for the mutant enzyme, while the KM is similar within the experimental error
additional information
optimization of enzyme production and enhancement of the enzyme activity compared to wild-type by codon engineering, overview
additional information
the recombinant Rha is optimized for production in a bioreactor for hydrolysis of rutin and naringin. Through high density-induced fermentation based on a glycerol feeding strategy in a 3-l bioreactor with fed-batch fermentation, the enzyme activity reaches 46.87 U/ml after 7 days of methanol induction/incubation, which is approximately 99 times higher than that produced in shaking flasks. This process offers a simple and effective approach for the large-scale production of alpha-L-rhamnosidase, method overview
additional information
Aspergillus niger CCTCC M 2018240
-
the recombinant Rha is optimized for production in a bioreactor for hydrolysis of rutin and naringin. Through high density-induced fermentation based on a glycerol feeding strategy in a 3-l bioreactor with fed-batch fermentation, the enzyme activity reaches 46.87 U/ml after 7 days of methanol induction/incubation, which is approximately 99 times higher than that produced in shaking flasks. This process offers a simple and effective approach for the large-scale production of alpha-L-rhamnosidase, method overview
-
additional information
Aspergillus niger JMU-TS528
-
optimization of enzyme production and enhancement of the enzyme activity compared to wild-type by codon engineering, overview
-
additional information
-
recombinant alpha-L-rhamnosidase BtRha from Bacteroides thetaiotaomicron strain VPI-5482 can convert epoetin C to produce icariin. From a combination of beta-D-xylosidase BbXyl (EC 3.2.1.37), which can convert epimedin B and epimedin C into icariin, and BtRha, the conversion of epimedium total flavonoids in vitro and in vivo to obtain product icariin is catalyzed. Under optimal conditions, in vitro hydrolysis of 5 g/l of total flavonoids of epimedium eventually yield a concentration of icariin of 678.1 micromol/l. To explore the conversion of total flavonoids of epimedium in vivo. Under the optimal conditions, the yield of icariin reaches 97.27 micromol/l when the total flavonoid concentration of epimedium is 1 g/l. Method optimization, overview. The optimum temperature for conversion of epimedin C by rhamnosidase BtRha is 55? and the optimum pH is 5.5, the final concentration of 1 g/l epimedin C is used as substrate and the final concentration of 3.6 U/ml of BtRha enzyme is reacted at 55?, pH 5.5 for 4 h. The conversion rate is 90.5%
additional information
-
recombinant alpha-L-rhamnosidase BtRha from Bacteroides thetaiotaomicron strain VPI-5482 can convert epoetin C to produce icariin. From a combination of beta-D-xylosidase BbXyl (EC 3.2.1.37), which can convert epimedin B and epimedin C into icariin, and BtRha, the conversion of epimedium total flavonoids in vitro and in vivo to obtain product icariin is catalyzed. Under optimal conditions, in vitro hydrolysis of 5 g/l of total flavonoids of epimedium eventually yield a concentration of icariin of 678.1 micromol/l. To explore the conversion of total flavonoids of epimedium in vivo. Under the optimal conditions, the yield of icariin reaches 97.27 micromol/l when the total flavonoid concentration of epimedium is 1 g/l. Method optimization, overview. The optimum temperature for conversion of epimedin C by rhamnosidase BtRha is 55? and the optimum pH is 5.5, the final concentration of 1 g/l epimedin C is used as substrate and the final concentration of 3.6 U/ml of BtRha enzyme is reacted at 55?, pH 5.5 for 4 h. The conversion rate is 90.5%
-
additional information
engineering of the recombinant enzyme for production of isoquercitrin from rutin, optimised conditions are pH 6.0, 50°C, 0.6 U/ml alpha-L-rhamnosidase, and 30 mM rutin, the recombinant enzyme produces 30 mM isoquercitrin in 2 h with a 100% conversion yield and productivity of 15 mM/h isoquercitrin
additional information
-
engineering of the recombinant enzyme for production of isoquercitrin from rutin, optimised conditions are pH 6.0, 50°C, 0.6 U/ml alpha-L-rhamnosidase, and 30 mM rutin, the recombinant enzyme produces 30 mM isoquercitrin in 2 h with a 100% conversion yield and productivity of 15 mM/h isoquercitrin
-
additional information
-
engineering of the recombinant enzyme for production of isoquercitrin from rutin, optimised conditions are pH 6.0, 50°C, 0.6 U/ml alpha-L-rhamnosidase, and 30 mM rutin, the recombinant enzyme produces 30 mM isoquercitrin in 2 h with a 100% conversion yield and productivity of 15 mM/h isoquercitrin
-
additional information
-
engineering of the recombinant enzyme for production of isoquercitrin from rutin, optimised conditions are pH 6.0, 50°C, 0.6 U/ml alpha-L-rhamnosidase, and 30 mM rutin, the recombinant enzyme produces 30 mM isoquercitrin in 2 h with a 100% conversion yield and productivity of 15 mM/h isoquercitrin
-
additional information
a highly flexible region is identified by molecular dynamics (MD), computational protein design (Rosetta) is used to increase rigidity and favorable interactions of residues in highly flexible regions. MD results show that five regions have the highest flexibilities and are selected for design by Rosetta. Mutational improvement of the enzyme for higher stability
additional information
-
a highly flexible region is identified by molecular dynamics (MD), computational protein design (Rosetta) is used to increase rigidity and favorable interactions of residues in highly flexible regions. MD results show that five regions have the highest flexibilities and are selected for design by Rosetta. Mutational improvement of the enzyme for higher stability
-
additional information
-
a highly flexible region is identified by molecular dynamics (MD), computational protein design (Rosetta) is used to increase rigidity and favorable interactions of residues in highly flexible regions. MD results show that five regions have the highest flexibilities and are selected for design by Rosetta. Mutational improvement of the enzyme for higher stability
-
additional information
-
a highly flexible region is identified by molecular dynamics (MD), computational protein design (Rosetta) is used to increase rigidity and favorable interactions of residues in highly flexible regions. MD results show that five regions have the highest flexibilities and are selected for design by Rosetta. Mutational improvement of the enzyme for higher stability
-
additional information
-
a highly flexible region is identified by molecular dynamics (MD), computational protein design (Rosetta) is used to increase rigidity and favorable interactions of residues in highly flexible regions. MD results show that five regions have the highest flexibilities and are selected for design by Rosetta. Mutational improvement of the enzyme for higher stability
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 11
24 h, 4°C, more than 45% of its enzymatic activity is retained
3 - 5
3 - 9
5 - 8
stable in the pH range 5.0-8.0 at 45°C for 4 h over 60%
5.5 - 10.5
over 80% residual enzyme activity of purified recombinant AtRha is maintained
5.5 - 9
6
purified recombinant His-tagged enzyme, 70% activity remaining after 120 min
7
purified recombinant His-tagged enzyme, 50% activity remaining after 120 min
8
purified recombinant His-tagged enzyme, 30% activity remaining after 120 min
8.6 - 9
the activity of BtRha78A is enhanced significantly after the incubation in alkaline environment. The enzyme retains 142% and 133% of initial activity after the incubation of 1 h at 40 °C in 50 mM glycine-NaOH buffer (pH 8.6 and pH 9.0), respectively
3 - 5
purified recombinant His-tagged enzyme, over 80% activity remaining after 120 min
3 - 9
the stability of isoform RhaB2 is lower than that of isoform RhaB1, with 80-85% enzymatic activity from pH 5.0 to 7.0, and only 17% and 12% at pH 3.0 and 9.0, respectively
3 - 9
isoform RhaB1 remains active over a broad range of pH values, showing 90-100% remaining relative activities from pH 4.0 to 7.5, and over 40% at pH 3 and 9, after 5 h at 37°C
5
1 h, 40 min, enzyme retains 75% of its initial activity
5.5 - 9
1 h, 40°C, more than 95% of the activity is retained
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
30 - 50
30 - 70
half-lives of the purified recombinant enzyme are 138, 78, 50, 13, and 7 h at 30, 40, 50, 60, and 70°C, respectively, at pH 6.0
40
40 - 60
-
at low enzyme concentration, activity rapidly decreases within the first 30 min incubation time but afterwards remains stable at about 45% of the initial value for 5 h. Addition of bovine serum albumine or increasing enzyme concentration up to 0.1 g/l renders the enzyme stable for 5 h without initial losses of activity
45 - 55
-
purified extracellular enzyme, pH 4.0-6.0, completely stable for 3 h
50
55
55 - 65
isoform RhaB2 retains 43% and 25% activity after 5 h incubation at 55°C and 65°C, respectively
60
60 - 70
-
purified extracellular enzyme, pH 4.0-6.0, 50-80% activity remaining after 90 min
60 - 75
purified recombinant AtRha is highly stable at 60°C maintaining over 80% of its initial activity after 6 h and 60% after 14 h. At 65°C, AsRha retains 15% of residual enzyme activity after 2 h. The recombinant enzyme maintains more than 60% activity at 65°C after 2 h, but activity significantly decreases above 70°C during 20 min and is completely lost after 80 min at 75°C
65
70
75
80
90
additional information
30 - 50
purified recombinant His-tagged enzyme, over 80% activity remaining after 120 min
50
-
2 h, 85% residual activity, inactivation is completely reversible, rhamnose and naringin protect
50
free enzyme, less than 50% loss of activityafter 3 h
60
purified recombinant His-tagged enzyme, 75% activity remaining after 120 min
60
-
1 h, enzyme retained more than 90% of its initial activity. It retains more than 80% of its initial activity after incubation for 2 h and does not further lose activity after treatment for 24 h
60
-
2 h, 70% residual activity, inactivation is completely reversible, rhamnose and naringin protect
65
half-life: 127.9 min without sorbitol, 5803 min in presence of 2.0 M sorbitol
70
T1/2: 6.35 min (mutant enzyme V529A), 4.35 min (wild-type enzyme)
70
purified recombinant His-tagged enzyme, 15% activity remaining after 120 min
70
half-life: 18.2 min without sorbitol, 313.7 min in presence of 2.0 M sorbitol. Half-life and activation free energy are increased by 17.2fold and 8.2 kJ/mol, respectively in presence of 2.0 M sorbitol
70
half-life: 19 min (wild-type enzyme), 39.8 min (mutant enzyme D594Q), 43.1 min (mutant enzyme D594Q/G827K)
70
-
the stability of alpha-L-rhamnosidase at 70°C increases twofold in the presence of 20-40% glycerol and 2.3fold in the presence of 4 M sorbitol, pH 5.0
75
half-life: 1.8 min without sorbitol, 54.6 min in presence of 2.0 M sorbitol. 2.0 M sorbitol prolonges the half-life 30.3fold
75
-
purified extracellular enzyme, pH 4.0-6.0, with temperature rise up to 75°C in 60 min, the activity decreases by 50%, and after 2.5 h of incubation under these conditions, no more than 5% of the initial activity remains
80
purified recombinant His-tagged enzyme, inactivation after 100 min
80
R4P072
purified recombinant enzyme, 98.1% activity remaining after 6 h, 73.0% residual activity after 12 h of incubation
80
purified recombinant enzyme, 91.0% activity remaining after 6 h, 68.5% residual activity after 12 h of incubation
90
R4P072
purified recombinant enzyme, 47.1% activity remaining after 6 h, 14.3.0% residual activity after 12 h of incubation
90
purified recombinant enzyme, 3.0% activity remaining after 6 h, 0.1% residual activity after 12 h of incubation
additional information
the alpha-L-rhamnosidase displays first-order kinetics for thermal inactivation
additional information
-
glycerol and glutaraldehyde stabilize the enzyme against thermal denaturation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of bovine serum albumine or increasing enzyme concentration up to 0.1 g/l renders the enzyme stable for 5 h without initial losses of activity
-
enzyme immobilised onto kappa-carrageenan beads surface can be recycled for 10 reactions, 90% yield retained
glycerol and glutaraldehyde stabilize the enzyme, while sorbitol does not. The formation of cross-links between amino groups of a protein with the help of glutaraldehyde can lead to the fixation of the active conformation of the molecule and the formation of aggregates with increased stability compared to native enzymes
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
F6IEX3
10% acetone, 50 mM MOPS, pH 6.9, 6.73% residual activity. Complete loss of activity in 50% acetone
DMSO
Ethanol
Methanol
DMSO
F6IEX3
10% DMSO, in 50 mM MOPS, pH 6.9, 66.29% residual activity. Complete loss of activity in 50% DMSO
DMSO
35% inhibition of enzyme activity at 10% v/v, 75% inhibition at 20% v/v
DMSO
-
35% inhibition of enzyme activity at 10% v/v, 75% inhibition at 20% v/v
-
Ethanol
F6IEX3
10% ethanol, 50 mM MOPS, pH 6.9, 66.52% residual activity. Complete loss of activity in 50% ethanol
Ethanol
40% inhibition of enzyme activity at 10% v/v, 70% inhibition at 20% v/v
Ethanol
-
40% inhibition of enzyme activity at 10% v/v, 70% inhibition at 20% v/v
-
Methanol
20% inhibition of enzyme activity at 10% v/v, 50% inhibition at 20% v/v
Methanol
-
20% inhibition of enzyme activity at 10% v/v, 50% inhibition at 20% v/v
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
3-5°C, pH 3.5, potassium hydrogen phthalate /HCl buffer, immobilized enzyme, 1 year, 10-15% loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap chelating column chromatography, gel filtration
native and recombinant proteins, gel filtration, SDS-PAGE
Q93RE7
native enzyme 27fold from culture supernatant by ammonium sulfate fractionation, dialysis, and gel filtration, followed by anion exchange chromatography, and dialysis
-
native enzyme 29fold from cell extract by ammonium sulfate fractionation, dialysis, PEG 6000 extraction, and gel filtration, followed by ulatrfiltration, another step of anion exchange chromatography, and dialysis, to homogeneity
-
native enzyme from strain FFDCL-90, by ammonium sulfate fractionation and ion exchange chromatography
-
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21 Star by immobilied metal affinity chromatography and heat treatment at 55°C
R4P072
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21 Star by immobilized metal affinity chromatography and heat treatment at 55C
recombinant enzyme 63fold from Escherichia coli by heat treatment at 60°C, hydrophobic interaction and ion exchange chromatography
recombinant enzyme 85fold from Escherichia coli by heat treatment at 60°C, hydrophobic interaction and ion exchange chromatography
recombinant extracellular enzyme from Pichia pastoris strain KM71H culture supernatant by ammonium sulfate fractionation, dialysis, anion exchange chromatgraphy, and again dialysis
recombinant extracellular His-tagged enzyme from culture supernatant of Aspergillus niger strain 3.350 by ultrafiltration and nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickell affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21 CodonPlus cell free extract by nickel affinity chromatography
-
recombinant His6-tagged isozyme Ram1 from Escherichia coli by immobilized metal affinity chromatography and dialysis
recombinant His6-tagged isozyme Ram2 from Escherichia coli by immobilized metal affinity chromatography and dialysis
recombinant secreted enzyme from Pichia pastoris strain GS115 cell culture supernatant by ammonium sulfate fractionation, desalting gel filtration, and ultrafiltration
recombinant wild-type and mutant enzymes from Pichia pastoris strain KM71H cell-free culture supernatant by anion exchange chromatography and gel filtration
-
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21 Star by immobilized metal affinity chromatography and heat treatment at 55C
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21 Star by immobilized metal affinity chromatography and heat treatment at 55C
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21 Star by immobilized metal affinity chromatography and heat treatment at 55C
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B834-DE3 containing pET3a-RhaB plasmid
Q93RE7
expressed in Escherichia coli BL21-DE3 pRIL cells, recombinant strain of Echerichia coli carrying the rhmA gene from Thermomicrobia bacterium, immobilization on Ca2+ alginate beads and packaging the beads onto a column to design a bioreactor for production of rhamnose from naringin
expressed in Escherichia coli strain HMS174-DE3, transformation with mutant plasmids, pD567N, pE572Q, pD579N, or pE841Q for mutant generation
Q93RE7
expression in Escherichia coli
expression in Escherichia coli, gene has no homology to other glycoside hydrolases
-
expression in Pichia pastoris
expression of alpha-L-rhamnosidase in Pichia pastoris and Kluyveromyces lactis achieves high protein yields of up to 17.6 U/ml and 30.6 U/ml
gene alpha-Rha, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, recombinant expression of the enzyme from linearized plasmid pPICZalphaA-AtRha in Pichia pastoris strain KM71H, the enzyme is secreted. 1000 U/ml enzyme activity are achieved at day 12
gene AorhaA, recombinant expression of wild-type and mutant enzymes in Pichia pastoris strain KM71H from vector pPICZalphaC-rhaA containing the alpha-factor secretion signal sequence of Saccharomyces cerevisiae, the recombinant enzymes are secreted
-
gene Athe_2581, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21 Star
gene cloning and codon optimization, recombinant enzyme expression in Pichia pastoris strain GS115 from pPIC9K vector
gene Cst_c00400, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21 Star
gene CTN_1495, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21 Star
gene ram1, recombinant expression of C-terminally His6-tagged isozyme Ram1 in Escherichia coli
gene ram2, recombinant expression of C-terminally His6-tagged isozyme Ram2 in Escherichia coli
gene rha, cloning and DNA and amino acid sequence determination and analysis, sequence comparisons, cloning and recombinant enzyme expression in Pichia pastoris strain GS115, subcloning in Escherichia coli strain JM109
gene rha, recombinant enzyme expression in Pichia pastoris strain GS115, the enzyme is secreted
gene rha, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21
gene rha, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 CodonPlus
-
gene rha-n1, cloning and recombinant His-tagged expression in Aspergillus niger strain 3.350 via transformation method using Agrobacterium tumefaciens strain AGL-1, the enzyme is secreted. Subcloning in Escherichia coli strain DH5alpha
gene rhaM, contsruction of a genomic library, DNA and mino acid sequence determination and analysis, expression in Escherichia coli
gene rhmA, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
gene rhmB, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
gene Tmari_1078, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21 Star
R4P072
recombinant enzyme epression in Pichia pastoris (Komagataella phaffii ) strain GS115 including methanol-inducible fermentation, an off-flavor is produced by Pichia pastoris strains during protein overexpression which has strong sweaty and moderate metallic and plastic notes. Tetramethylpyrazine, 2,4-di-tert-butylphenol, isovaleric acid, and 2-methylbutyric acid, are identified to be major contributors to the sweaty note. Dodecanol and 2-acetylbutyrolactone are identified to be contributors to the metallic and plastic notes, respectively, via sensory evaluation, gas chromatography-mass spectrometry, gas chromatography, and omission test, detailed overview
-
recombinant enzyme expression in Escherichia coli strain BL21
recombinant enzyme expression in Escherichia coli strain BL21(DE3)
recombinant enzyme expression in Pichia pastoris strain GS115
the recombinant protein is fused to a C-terminal His-tag and expressed in Escherichia coli BL21(DE3)
F6IEX3
recombinant enzyme expression in Escherichia coli strain BL21(DE3)
recombinant enzyme expression in Escherichia coli strain BL21(DE3)
recombinant enzyme expression in Escherichia coli strain BL21(DE3)
recombinant enzyme expression in Escherichia coli strain BL21(DE3)
recombinant enzyme expression in Escherichia coli strain BL21(DE3)
recombinant enzyme expression in Escherichia coli strain BL21(DE3)
F6IEX3
recombinant enzyme expression in Escherichia coli strain BL21(DE3)
R4P072
recombinant enzyme expression in Escherichia coli strain BL21(DE3)
recombinant enzyme expression in Pichia pastoris strain GS115
recombinant enzyme expression in Pichia pastoris strain GS115
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme activity is downregulated by D-glucose
the enzyme activity is upregulated by L-rhamnose
the specific activity of rhamnosidase was 0.57 U/mg in LB medium with 0.1 mM isopropyl beta-D-thiogalactoside induction at 28 C for 8 h
the enzyme activity is downregulated by D-glucose
the specific activity of rhamnosidase was 0.57 U/mg in LB medium with 0.1 mM isopropyl beta-D-thiogalactoside induction at 28 C for 8 h
the specific activity of rhamnosidase was 0.57 U/mg in LB medium with 0.1 mM isopropyl beta-D-thiogalactoside induction at 28 C for 8 h
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
alpha-L-rhamnosidases have been used for plant and bacterial polysaccharide, glycoside, and glycolipid structural analysis
biotechnology
degradation
recombinant rhamnosidase is thermostable and highly active for naringin hydrolysis up to more than 77%, thus producing L-rhamnose and prunin from citrus peel waste
drug development
food industry
industry
nutrition
pharmacology
alpha-L-rhamnosidase is an important enzyme with applications in the pharmaceutical industries because it can release terminal L-rhamnose residues from various natural products. The D594Q and G827K/D594Q mutant enzymes are more suitable for the industrial processes of isoquercitrin preparation than the wild-type enzyme
synthesis
additional information
biotechnology
-
enzyme efficiently releases monoterpenols from an aroma precursor from muscat grape juice
biotechnology
F6IEX3
potential use as a biocatalyst for diverse biotechnological applications
drug development
the characteristics (good thermostability, wide range of pH-stability with the optimum pH of 5.0 and temperature of 60°C, not greatly affected by representative metal ions, excellent tolerance abilities against glucose and ethanol) of the enzyme suggest that it should be considered a potential new biocatalyst for food and drug industrial applications
drug development
Aspergillus niger JMU-TS528
-
the characteristics (good thermostability, wide range of pH-stability with the optimum pH of 5.0 and temperature of 60°C, not greatly affected by representative metal ions, excellent tolerance abilities against glucose and ethanol) of the enzyme suggest that it should be considered a potential new biocatalyst for food and drug industrial applications
-
food industry
-
the purified enzyme has potential for enhancement of wine aroma
food industry
the enzyme can remove the bitter taste of naringin from citrus juices. Improvement of thermostabilty can promote the practical value of the enzyme in citrus juice processing
food industry
-
the enzyme is used to enhance wine aromas or to debitter citrus juices by releasing L-rhamnose
food industry
with the enhanced thermostability, the mutant enzyme, K406R/K573R, has potentially broadened the applications of alpha-L-rhamnosidase in food processing industry
food industry
the characteristics (good thermostability, wide range of pH-stability with the optimum pH of 5.0 and temperature of 60°C, not greatly affected by representative metal ions, excellent tolerance abilities against glucose and ethanol) of the enzyme suggest that it should be considered a potential new biocatalyst for food and drug industrial applications
food industry
the enzyme can efficiently remove naringin from pomelo juice without changing its aroma. It is desirable for debittering citrus juice thereby improving the quality of juice
food industry
alpha-L-rhamnosidase is an important enzyme with applications in the food industries because it can release terminal L-rhamnose residues from various natural products. The D594Q and G827K/D594Q mutant enzymes are more suitable for the industrial processes of isoquercitrin preparation than the wild-type enzyme
food industry
efficient and cost-effective enzymatic production method for preparation of the high-valued natural sweetener trilobatin is developed by the combination of hydrogenation and enzymatic hydrolysis reactions with alpha-L-rhamnosidase as the catalyst in aqueous medium. This technology is adopting the cheap and largely available citrus flavanone naringin as the starting material for trilobatin synthesis, and the present enzymatic technology is possibly utilised by commercial for scale-up production. The production is a straightforward two-step process, in which naringin is hydrogenated into naringin dihydrochalcone and followed by removal of the rhamnosyl group of naringin dihydrochalcone by enzymatic hydrolysis using immobilised alpha-L-rhamnosidase as the catalyst. Under optimised conditions, an overall yield of 96% is achieved with a very low loading of alpha-L-rhamnosidase catalyst at 60 °C in a neutral aqueous buffer solution within 2 h. The immobilised alpha-L-rhamnosidase catalyst can be recycled for 10 reactions (90% yield retained)
food industry
-
the enzyme exhibits transglycosylating activity, which can synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. The enzyme has potential value for glycoside synthesis in the food industry
food industry
Aspergillus terreus alpha-L-rhamnosidase specifically hydrolyses the glycosidic linkage of dulcoside A (the bitterest compounds in steviol glycoside mixtures), and converts it to rubusoside. During a 12 h biotransformation, the dulcoside A from crude leaf extracts is completely converted by recombinant alpha-L-rhamnosidase from Aspergillus terreus into rubusoside. This process offers a promising approach for reducing the bitterness of steviol glycoside mixtures
food industry
the enzyme is used for debittering of citrus juices in the food industry
food industry
-
alpha-L-rhamnosidases play a role in enhancing the aroma of grape juices and derived beverages. They are also used in citrus juices to remove naringin-caused bitterness
food industry
-
the enzyme is useful for enzymatic deramnosylation of flavonoids, a convenient tool for improving the quality of citrus juices. The enzyme might be an effective tool for transformation of bioflavonoids in food industry
food industry
-
the enzyme is used for debittering of citrus juices in the food industry
-
food industry
-
the enzyme is used for debittering of citrus juices in the food industry
-
food industry
Aspergillus niger JMU-TS528
-
the enzyme can remove the bitter taste of naringin from citrus juices. Improvement of thermostabilty can promote the practical value of the enzyme in citrus juice processing
-
food industry
Aspergillus niger JMU-TS528
-
with the enhanced thermostability, the mutant enzyme, K406R/K573R, has potentially broadened the applications of alpha-L-rhamnosidase in food processing industry
-
food industry
Aspergillus niger JMU-TS528
-
the characteristics (good thermostability, wide range of pH-stability with the optimum pH of 5.0 and temperature of 60°C, not greatly affected by representative metal ions, excellent tolerance abilities against glucose and ethanol) of the enzyme suggest that it should be considered a potential new biocatalyst for food and drug industrial applications
-
food industry
Aspergillus niger JMU-TS528
-
efficient and cost-effective enzymatic production method for preparation of the high-valued natural sweetener trilobatin is developed by the combination of hydrogenation and enzymatic hydrolysis reactions with alpha-L-rhamnosidase as the catalyst in aqueous medium. This technology is adopting the cheap and largely available citrus flavanone naringin as the starting material for trilobatin synthesis, and the present enzymatic technology is possibly utilised by commercial for scale-up production. The production is a straightforward two-step process, in which naringin is hydrogenated into naringin dihydrochalcone and followed by removal of the rhamnosyl group of naringin dihydrochalcone by enzymatic hydrolysis using immobilised alpha-L-rhamnosidase as the catalyst. Under optimised conditions, an overall yield of 96% is achieved with a very low loading of alpha-L-rhamnosidase catalyst at 60 °C in a neutral aqueous buffer solution within 2 h. The immobilised alpha-L-rhamnosidase catalyst can be recycled for 10 reactions (90% yield retained)
-
food industry
Aspergillus tubingensis JMU-TS529
-
the enzyme can efficiently remove naringin from pomelo juice without changing its aroma. It is desirable for debittering citrus juice thereby improving the quality of juice
-
food industry
Fusarium verticillioides MTCC-2088
-
the purified enzyme has potential for enhancement of wine aroma
-
food industry
Alternaria alternata SK37.001
-
the enzyme is used to enhance wine aromas or to debitter citrus juices by releasing L-rhamnose
-
food industry
Aspergillus oryzae NL-1
-
the enzyme exhibits transglycosylating activity, which can synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. The enzyme has potential value for glycoside synthesis in the food industry
-
food industry
-
the enzyme is used for debittering of citrus juices in the food industry
-
food industry
-
the enzyme is used for debittering of citrus juices in the food industry
-
food industry
Penicillium tardum 3024
-
the enzyme is useful for enzymatic deramnosylation of flavonoids, a convenient tool for improving the quality of citrus juices. The enzyme might be an effective tool for transformation of bioflavonoids in food industry
-
industry
the enzyme is a promising alternative biocatalyst for industrial applications due to good pH stability, relatively high thermostability and tolerance to low concentration of alcohols
industry
stable alpha-L-rhamnosidase with cleaving terminal alpha-L-rhamnose activity has great potential in industrial application. Enhancing the thermostability of alpha-L-rhamnosidase from Aspergillus terreus makes it a good candidate for industrial processes of isoquercitrin preparation
industry
the enzyme is used for flavonoid derhamnosylation in the pharmaceutical industry
industry
-
the enzyme is a promising alternative biocatalyst for industrial applications due to good pH stability, relatively high thermostability and tolerance to low concentration of alcohols
-
industry
-
the enzyme is used for flavonoid derhamnosylation in the pharmaceutical industry
-
industry
-
the enzyme is used for flavonoid derhamnosylation in the pharmaceutical industry
-
industry
-
the enzyme is used for flavonoid derhamnosylation in the pharmaceutical industry
-
industry
-
the enzyme is used for flavonoid derhamnosylation in the pharmaceutical industry
-
nutrition
alpha-L-rhamnosidases are used in wine production
nutrition
-
production of bioavailable flavonoid glucosides in fruit juices and green tea by use of fungal alpha-L-rhamnosidases RhaA and RhaB from Aspergillus aculeatus
nutrition
application in fruit juice and wine industry, bioreactor design for production of rhamnose from natural flavinoids such as naringin
nutrition
-
production of bioavailable flavonoid glucosides in fruit juices and green tea by use of fungal alpha-L-rhamnosidases RhaA and RhaB from Aspergillus aculeatus
-
synthesis
immobilization of recombinant enzyme on Ca2+ alginate beads. Immobilization enables its reutilization up to 9 hydrolysis batches without an appreciable loss in activity
synthesis
adding sorbitol has great potential to promote enzymatic conversion of rutin to isoquercitrin production. Isoquercitrin has several biological activities, including anti-mutagenesis, anti-virus, anti-hypertensive, anti-proliferative effects, lipid peroxidation, oxidative-stress protection as well as other pharmacological effects
synthesis
-
a wild-type alpha-L-rhamnosidase from Alternaria sp. L1 can synthesize rhamnose-containing chemicals through reverse hydrolysis reaction with inexpensive rhamnose as glycosyl donor
synthesis
potential use of Ram2 to selectively produce isoquercetin
synthesis
-
the enzymatic hydrolysis method optimized for the enzyme to produce icariin from epimedin C can be used for the industrialized production of icariin. The enzyme can also cleave the alpha-1,2 glycosidic linkage between glucoside and rhamnoside in naringin and neohesperidin, which could be applicable in other biotechnological processes
synthesis
the purified enzyme is used as a biocatalyst for the transformation of flavonoids (rutin, hesperidin, and naringin) to obtain the flavonoid monoglycosides (isoquercetin, hesperetin-7-O-glucoside, and pulunin)
synthesis
alpha-L-rhamnosidase from Alternaria sp. L1, RhaL1, is used to perform one-step rhamnosylation of anticancer drugs, including 2'-deoxy-5-fluorouridine (FUDR), cytosine arabinoside (Ara C), and hydroxyurea (Hydrea). Maximum yields of each rhamnosylated drugs are 57.7 mmol for rhamnosylated Ara C, 68.6 mmol for rhamnosylated Hydrea, and 42.2 mmol for rhamnosylated FUDR. The rhamnosylated drugs exhibit little cytotoxic effects on cancer cells, but efficiently restore cytotoxic activity when incubated with exogenous alpha-L-rhamnosidase, allowing their potential applications in the enzyme-activated prodrug system. The rhamnose moiety can mediate the specific internalization of rhamnosylated compounds into cancer cells, which greatly facilitated their applications for cancer-targeting drug delivery
synthesis
-
enzyme RHA-P is a potential catalyst to increase the bioavailability of rhamnosylated natural compounds
synthesis
application of the enzyme in the production of isoquercitrin from rutin
synthesis
enzyme AtRha can hydrolyze icariin containing the alpha-1 rhamnoside linkage. alpha-L-Rhamnosidase AtRha and beta-glucosidase TthBg3 show excellent selectivity to cleave the rhamnose at the 3rd position and the glucosyl at the C-7 group of icariin, which establishes an effective and green method to produce the more pharmacological active icaritin. After a two-stage transformation under optimized conditions, 0.5 g/l of icariin is transformed into 0.25 g/l of icaritin, with a corresponding molar conversion rate of 91.2%
synthesis
-
application of the enzyme in the production of isoquercitrin from rutin
-
synthesis
Lactiplantibacillus plantarum NCIMB 8826
-
potential use of Ram2 to selectively produce isoquercetin
-
synthesis
Lactiplantibacillus plantarum ATCC BAA-793
-
potential use of Ram2 to selectively produce isoquercetin
-
synthesis
-
the purified enzyme is used as a biocatalyst for the transformation of flavonoids (rutin, hesperidin, and naringin) to obtain the flavonoid monoglycosides (isoquercetin, hesperetin-7-O-glucoside, and pulunin)
-
synthesis
-
application of the enzyme in the production of isoquercitrin from rutin
-
synthesis
Aspergillus niger FGSC A1513
-
the purified enzyme is used as a biocatalyst for the transformation of flavonoids (rutin, hesperidin, and naringin) to obtain the flavonoid monoglycosides (isoquercetin, hesperetin-7-O-glucoside, and pulunin)
-
synthesis
Aspergillus niger ATCC MYA-4892
-
the purified enzyme is used as a biocatalyst for the transformation of flavonoids (rutin, hesperidin, and naringin) to obtain the flavonoid monoglycosides (isoquercetin, hesperetin-7-O-glucoside, and pulunin)
-
synthesis
-
application of the enzyme in the production of isoquercitrin from rutin
-
synthesis
Aspergillus terreus CCF3059
-
enzyme AtRha can hydrolyze icariin containing the alpha-1 rhamnoside linkage. alpha-L-Rhamnosidase AtRha and beta-glucosidase TthBg3 show excellent selectivity to cleave the rhamnose at the 3rd position and the glucosyl at the C-7 group of icariin, which establishes an effective and green method to produce the more pharmacological active icaritin. After a two-stage transformation under optimized conditions, 0.5 g/l of icariin is transformed into 0.25 g/l of icaritin, with a corresponding molar conversion rate of 91.2%
-
synthesis
Papiliotrema laurentii ZJU-L07
-
the enzymatic hydrolysis method optimized for the enzyme to produce icariin from epimedin C can be used for the industrialized production of icariin. The enzyme can also cleave the alpha-1,2 glycosidic linkage between glucoside and rhamnoside in naringin and neohesperidin, which could be applicable in other biotechnological processes
-
additional information
alpha-L-rhamnosidase is widely used in food processing and pharmaceutical preparation
additional information
Aspergillus niger JMU-TS528
-
alpha-L-rhamnosidase is widely used in food processing and pharmaceutical preparation
-
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REF.
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Aspergillus niger (R9W5L0), Aspergillus niger JMU-TS528 (R9W5L0)
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Aspergillus oryzae, Aspergillus oryzae NL-1
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Aspergillus tubingensis (A0A1B2K4A7), Aspergillus tubingensis JMU-TS529 (A0A1B2K4A7)
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Klebsiella oxytoca (A0A0J9X262), Klebsiella oxytoca
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Aspergillus niger (A0A3F3R7H5), Aspergillus niger CCTCC M 2018240 (A0A3F3R7H5)
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Aspergillus niger (A2Q947), Aspergillus niger ATCC MYA-4892 (A2Q947), Aspergillus niger CBS 513.88 (A2Q947), Aspergillus niger FGSC A1513 (A2Q947)
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alpha-L-Rhamnosidase from Penicillium tardum and its application for biotransformation of Citrus rhamnosides
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Penicillium tardum, Penicillium tardum 3024
brenda
Xu, L.; Liu, X.; Li, Y.; Yin, Z.; Jin, L.; Lu, L.; Qu, J.; Xiao, M.
Enzymatic rhamnosylation of anticancer drugs by an beta-L-rhamnosidase from Alternaria sp. L1 for cancer-targeting and enzyme-activated prodrug therapy
Appl. Microbiol. Biotechnol.
103
7997-8008
2019
Alternaria sp. L1 (H6UY33)
brenda
Terry, B.; Ha, J.; De Lise, F.; Mensitieri, F.; Izzo, V.; Sazinsky, M.H.
The crystal structure and insight into the substrate specificity of the alpha-L rhamnosidase RHA-P from Novosphingobium sp. PP1Y
Arch. Biochem. Biophys.
679
108189
2020
Novosphingobium sp. PP1Y
brenda
Su, J.; Wu, T.; Cao, S.; Pei, J.; Zhao, L.
Screening and characterization of a beta-xylosidase from Bifidobacterium breve K-110 and its application in the biotransformation of the total flavonoids of epimedium to icariin with alpha-L-rhamnosidase
Bioorg. Chem.
132
106364
2023
Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron VPI-5482
brenda
Shin, K.C.; Seo, M.J.; Oh, D.K.; Choi, M.N.; Kim, D.W.; Kim, Y.S.; Park, C.S.
Cloning and characterization of alpha-L-rhamnosidase from Chloroflexus aurantiacus and its application in the production of isoquercitrin from rutin
Biotechnol. Lett.
41
419-426
2019
Chloroflexus aurantiacus (A9WDK5), Chloroflexus aurantiacus ATCC 29366 (A9WDK5), Chloroflexus aurantiacus DSM 635 (A9WDK5), Chloroflexus aurantiacus J-10-fl (A9WDK5)
brenda
Li, Q.; Ge, L.; Zheng, D.; Zhang, X.; Zhao, L.
Screening and characterization of a GH78 alpha-L-rhamnosidase from Aspergillus terreus and its application in the bioconversion of icariin to icaritin with recombinant beta-glucosidase
Enzyme Microb. Technol.
153
109940
2022
Aspergillus terreus (I0AZ41), Aspergillus terreus CCF3059 (I0AZ41)
brenda
Ferreira-Lazarte, A.; Plaza-Vinuesa, L.; de Las Rivas, B.; Villamiel, M.; Munoz, R.; Moreno, F.J.
Production of ?-rhamnosidases from Lactobacillus plantarum WCFS1 and their role in deglycosylation of dietary flavonoids naringin and rutin
Int. J. Biol. Macromol.
193
1093-1102
2021
Lactiplantibacillus plantarum (F9UUD8), Lactiplantibacillus plantarum (F9UUE0), Lactiplantibacillus plantarum NCIMB 8826 (F9UUD8), Lactiplantibacillus plantarum NCIMB 8826 (F9UUE0), Lactiplantibacillus plantarum ATCC BAA-793 (F9UUD8), Lactiplantibacillus plantarum ATCC BAA-793 (F9UUE0)
brenda
Lou, H.; Liu, X.; Liu, S.; Chen, Q.
Purification and characterization of a novel alpha-L-rhamnosidase from Papiliotrema laurentii ZJU-L07 and its application in production of icariin from epimedin C
J. Fungi (Basel)
8
644
2022
Papiliotrema laurentii, Papiliotrema laurentii ZJU-L07
brenda
Yao, Y.; Zheng, S.; Chi, S.; Chen, F.; Cai, N.; Cai, Z.; Li, Z.; Ni, H.
Characterization of the off-flavor from Pichia pastoris GS115 during the over-expression of a alpha-L-rhamnosidase
J. Ind. Microbiol. Biotechnol.
50
kuad035
2023
Aspergillus tubingensis
brenda
Ge, L.; Liu, Y.; Zhou, F.; Zhan, L.; Zhao, L.
Heterologous expression and characterization of a thermostable alpha-L-rhamnosidase from Thermoclostridium stercorarium subsp. thermolacticum DSM 2910 and its application in the biotransformation of rutin
J. Microbiol. Biotechnol.
33
1521-1530
2023
Thermoclostridium stercorarium subsp. thermolacticum (A0A1B1YCF6), Thermoclostridium stercorarium subsp. thermolacticum DSM 2910 (A0A1B1YCF6)
brenda
Sitthiyotha, T.; Klaewkla, M.; Krusong, K.; Pichyangkura, R.; Chunsrivirot, S.
Computational design of Lactobacillus acidophilus alpha-L-rhamnosidase to increase its structural stability
PLoS ONE
17
e0268953
2022
Lactobacillus acidophilus (Q5FJ31), Lactobacillus acidophilus ATCC 700396 (Q5FJ31), Lactobacillus acidophilus N2 (Q5FJ31), Lactobacillus acidophilus NCFM (Q5FJ31), Lactobacillus acidophilus NCK56 (Q5FJ31)
brenda
Makabe, K.; Ishida, N.; Kanezaki, N.; Shiono, Y.; Koseki, T.
Aspergillus oryzae alpha-L-rhamnosidase crystal structure and insight into the substrate specificity
Proteins
92
236-245
2023
Aspergillus oryzae
brenda
Baudrexl, M.; Schwarz, W.H.; Zverlov, V.V.; Liebl, W.
Biochemical characterisation of four rhamnosidases from thermophilic bacteria of the genera Thermotoga, Caldicellulosiruptor and Thermoclostridium
Sci. Rep.
9
15924
2019
Thermotoga maritima (R4P072), Thermotoga neapolitana (B9K9N8), Caldicellulosiruptor bescii (B9MP87), Thermoclostridium stercorarium subsp. stercorarium (L7VK28), Thermotoga maritima DSM 3109 (R4P072), Thermotoga neapolitana DSM 4359 (B9K9N8), Thermotoga maritima ATCC 43589 (R4P072), Caldicellulosiruptor bescii DSM 6725 (B9MP87), Thermoclostridium stercorarium subsp. stercorarium DSM 8532 (L7VK28), Thermotoga maritima JCM 10099 (R4P072), Caldicellulosiruptor bescii ATCC BAA-1888 (B9MP87), Thermotoga maritima NBRC 100826 (R4P072), Thermotoga neapolitana ATCC 49049 (B9K9N8), Thermotoga neapolitana Z2706-MC24 (B9K9N8), Thermotoga neapolitana NBRC 107923 (B9K9N8), Thermotoga neapolitana NS-E (B9K9N8), Caldicellulosiruptor bescii KCTC 15123 (B9MP87), Caldicellulosiruptor bescii Z-1320 (B9MP87)
brenda
Pan, L.; Zhang, Y.; Zhang, F.; Wang, Z.; Zheng, J.
alpha-L-rhamnosidase production, properties, and applications
World J. Microbiol. Biotechnol.
39
191
2023
Alternaria sp. L1 (H6UY33), Aspergillus aculeatus (Q9C1M9), Aspergillus nidulans (I0J226), Aspergillus niger (R9W5L0), Aspergillus niger (A0A3F3R7H5), Aspergillus oryzae, Aspergillus tubingensis (A0A1B2K4A7), Bacillus sp. GL1 (Q93RE8), Bacillus sp. GL1 (Q93RE7), Bacteroides thetaiotaomicron (Q8A916), Bacteroides thetaiotaomicron VPI-5482 (Q8A916), Bifidobacterium breve, Bifidobacterium dentium (X2CNV1), Chloroflexus aurantiacus (A9WDK5), Chloroflexus aurantiacus J-10-fl (A9WDK5), Dictyoglomus thermophilum (B5YC64), Klebsiella oxytoca (A0A0H3HGQ6), Klebsiella oxytoca ATCC 8724 (A0A0H3HGQ6), Lactiplantibacillus plantarum (C4PG45), Lactiplantibacillus plantarum (C4PG47), Lactiplantibacillus plantarum (F9UUD8), Lactiplantibacillus plantarum NCIMB 8826 (F9UUD8), Lactobacillus acidophilus, Novosphingobium sp. PP1Y (F6IEX3), Paenibacillus odorifer, Pediococcus acidilactici (E0NEV1), Pediococcus acidilactici (E0NEK0), Sphingomonas paucimobilis (Q76LC4), Streptomyces avermitilis (Q82PP4), Talaromyces stollii, Thermoclostridium stercorarium (Q9S3L0), Thermotoga maritima (R4P072), Thermotoga petrophila (A5INB4), Xylaria polymorpha (H6V911), Aspergillus niger JMU-TS528 (R9W5L0), Bacteroides thetaiotaomicron ATCC 29148 (Q8A916), Bacteroides thetaiotaomicron CCUG 10774 (Q8A916), Bacteroides thetaiotaomicron DSM 2079 (Q8A916), Bacteroides thetaiotaomicron E50 (Q8A916), Bacteroides thetaiotaomicron JCM 5827 (Q8A916), Bacteroides thetaiotaomicron NCTC 10582 (Q8A916), Chloroflexus aurantiacus ATCC 29366 (A9WDK5), Chloroflexus aurantiacus DSM 635 (A9WDK5), Dictyoglomus thermophilum ATCC 35947 (B5YC64), Dictyoglomus thermophilum DSM 3960 (B5YC64), Dictyoglomus thermophilum H-6-12 (B5YC64), Klebsiella oxytoca BUCSAV 143 (A0A0H3HGQ6), Klebsiella oxytoca CCM 1901 (A0A0H3HGQ6), Klebsiella oxytoca DSM 4798 (A0A0H3HGQ6), Klebsiella oxytoca JCM 20051 (A0A0H3HGQ6), Klebsiella oxytoca KCTC 1686 (A0A0H3HGQ6), Klebsiella oxytoca NBRC 3318 (A0A0H3HGQ6), Klebsiella oxytoca NRRL B-199 (A0A0H3HGQ6), Lactiplantibacillus plantarum ATCC BAA-793 (F9UUD8), Lactiplantibacillus plantarum NCC245 (C4PG45), Lactiplantibacillus plantarum NCC245 (C4PG47), Paenibacillus odorifer DSM 15391, Pediococcus acidilactici DSM 20284 (E0NEV1), Pediococcus acidilactici DSM 20284 (E0NEK0), Sphingomonas paucimobilis FP2001 (Q76LC4), Streptomyces avermitilis ATCC 31267 (Q82PP4), Streptomyces avermitilis DSM 46492 (Q82PP4), Streptomyces avermitilis JCM 5070 (Q82PP4), Streptomyces avermitilis MA-4680 (Q82PP4), Streptomyces avermitilis NBRC 14893 (Q82PP4), Streptomyces avermitilis NCIMB 12804 (Q82PP4), Streptomyces avermitilis NRRL 8165 (Q82PP4), Thermotoga maritima ATCC 43589 (R4P072), Thermotoga maritima DSM 3109 (R4P072), Thermotoga maritima JCM 10099 (R4P072), Thermotoga maritima NBRC 100826 (R4P072), Thermotoga petrophila ATCC BAA-488 (A5INB4), Thermotoga petrophila DSM 13995 (A5INB4), Thermotoga petrophila RKU-1 (A5INB4), Aspergillus niger CCTCC M 2018240 (A0A3F3R7H5), Bifidobacterium breve ATCC 15700, Lactobacillus acidophilus DSM 9126, Talaromyces stollii CLY-6, Thermotoga petrophila JCM 10881 (A5INB4)
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