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Information on EC 3.2.1.125 - raucaffricine beta-glucosidase
for references in articles please use BRENDA:EC3.2.1.125
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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
3.2.1.125 raucaffricine beta-glucosidase
IUBMB Comments
Highly specific; some other ajmalan glucoside alkaloids are hydrolysed, but more slowly.
The enzyme appears in viruses and cellular organisms
- 3.2.1.125
- strictosidine
- serpentina
- rauvolfia
- indole
- ajmaline
-
monoterpenoid
-
glucosidases
- glycosides
-
deglucosylation
- hydrolases
- secologanin
- pharmacology
showSynonyms
raucaffricine-o-beta-d-glucosidase, raucaffricine glucosidase, raucaffricine beta-glucosidase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glucosidase, raucaffricine beta-
-
-
-
-
raucaffricine beta-D-glucosidase
-
-
-
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raucaffricine glucosidase
raucaffricine-O-beta-D-glucosidase
RG
additional information
raucaffricine glucosidase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
raucaffricine + H2O = D-glucose + vomilenine
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
raucaffricine beta-D-glucohydrolase
Highly specific; some other ajmalan glucoside alkaloids are hydrolysed, but more slowly.
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CAS REGISTRY NUMBER
COMMENTARY
102925-37-1
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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
1,2,19,20-tetrahydroraucaffricine + H2O
17-O-acetylnorajmaline + D-glucose
-
Substrates: 87% of activity compared to raucaffricine
Products: -
Products: -
?
1,2-(S)-dihydro-raucaffricine + H2O
2beta(R)-1,2-dihydrovomilenine + D-glucose
-
Substrates: 98% acivity compared to raucaffricine
Products: -
Products: -
?
1,2-dihydro-1-methylraucaffricine + H2O
acetic acid 3-ethylidene-4-hydroxy-13-methyl-1,3,4,7,8,13,13a,13b-octahydro-2H,6H-2,7-cyclo-6,8a-methano-pyrido[1',2':1,2]azepino[3,4-b]indol-8-yl ester + D-glucose
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Substrates: 36% of activity compared to raucaffricine
Products: -
Products: -
?
1,2-dihydroraucaffricine + H2O
?
Substrates: recombinant RG
Products: -
Products: -
?
1-methyl-1,2-dihydroraucaffricine + H2O
?
Substrates: recombinant RG
Products: -
Products: -
?
17-O-deacetyl-1,2-dihydroraucaffricine + H2O
3-ethylidene-1,3,4,7,8,13,13a,13b-octahydro-2H,6H-2,7-cyclo-6,8a-methano-pyrido[1',2':1,2]azepino[3,4-b]indole-4,8-diol + D-glucose
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Substrates: 95% of activity compared to raucaffricine
Products: -
Products: -
?
21-glucopyranosyl-hydroxysarpagan-17-al + H2O
?
Substrates: recombinant RG
Products: -
Products: -
?
21-glucopyranosyl-hydroxysarpagan-17-ol + H2O
?
Substrates: recombinant RG
Products: -
Products: -
?
5alpha-carboxystrictosidine + H2O
?
Substrates: recombinant RG
Products: -
Products: -
?
raucaffricine + H2O
vomilenine + D-glucose
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Substrates: -
Products: -
Products: -
?
secologanin + H2O
secologanin aglycone
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Substrates: 0.24% acivity compared to raucaffricine
Products: -
Products: -
?
strictosidine + H2O
strictosidine aglycone + D-glucose
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Substrates: 1.18% acivity compared to raucaffricine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with arbutin
Products: -
Products: -
?
1,2-dihydroraucaffricine + H2O
2beta(R)-1,2-dihydrovomilenine + D-glucose
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Substrates: 98% of activity compared to raucaffricine
Products: -
Products: -
?
1,2-dihydroraucaffricine + H2O
2beta(R)-1,2-dihydrovomilenine + D-glucose
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Substrates: -
Products: -
Products: -
?
raucaffricine + H2O
D-glucose + vomilenine
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Substrates: -
Products: the product vomilenine exists in aqueous solutions in an equilibrium of 21(R)- and 21(S)-vomilenine in a ratio of 3.4:1
Products: the product vomilenine exists in aqueous solutions in an equilibrium of 21(R)- and 21(S)-vomilenine in a ratio of 3.4:1
?
raucaffricine + H2O
D-glucose + vomilenine
Substrates: best substrate, highly specific enzyme
Products: -
Products: -
?
raucaffricine + H2O
D-glucose + vomilenine
-
Substrates: involved in the biosynthesis of alkaloids, e.g. ajmaline
Products: -
Products: -
?
raucaffricine + H2O
D-glucose + vomilenine
Substrates: specifically involved in alkaloid biosynthesis, e.g. ajmaline
Products: vomilene is a direct intermediate in ajmaline biosynthesis
Products: vomilene is a direct intermediate in ajmaline biosynthesis
?
raucaffricine + H2O
D-glucose + vomilenine
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Substrates: best substrate
Products: -
Products: -
?
raucaffricine + H2O
D-glucose + vomilenine
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Substrates: 100% activity
Products: -
Products: -
?
raucaffricine + H2O
D-glucose + vomilenine
Substrates: -
Products: -
Products: -
?
raucaffricine + H2O
D-glucose + vomilenine
Substrates: -
Products: -
Products: -
?
strictosidine + H2O
?
Substrates: only recombinant RG, no substrate of native RG
Products: -
Products: -
?
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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
raucaffricine + H2O
D-glucose + vomilenine
-
Substrates: involved in the biosynthesis of alkaloids, e.g. ajmaline
Products: -
Products: -
?
raucaffricine + H2O
D-glucose + vomilenine
Substrates: specifically involved in alkaloid biosynthesis, e.g. ajmaline
Products: vomilene is a direct intermediate in ajmaline biosynthesis
Products: vomilene is a direct intermediate in ajmaline biosynthesis
?
raucaffricine + H2O
D-glucose + vomilenine
Substrates: -
Products: -
Products: -
?
raucaffricine + H2O
D-glucose + vomilenine
Substrates: -
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-(bromobenzyl)-beta-D-gluco-1,5-deoxa-pyranosylamine
the inhibitor anchors exclusively in the catalytic active site by competition with appropriate enzyme substrates
N-(cyclohexyl)-beta-D-gluco-1,5-deoxa-pyranosylamine
the inhibitor anchors exclusively in the catalytic active site by competition with appropriate enzyme substrates
N-(cyclohexylmethyl)-beta-D-gluco-1,5-deoxa-pyranosylamine
the inhibitor anchors exclusively in the catalytic active site by competition with appropriate enzyme substrates
additional information
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D-glucono-1,5-lactone up to 1 M, phenylmethylsulfonyl fluoride up to 80 mM, EDTA up to 80 mM, iodoacetamide up to 80 mM, strictosidine or amygdalin up to 50 mM, mannitol up to 1 M are no inhibitors
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
Raucaffricine
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wild type enzyme, pH and temperature not specified in the publication
1.8
strictosidine
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wild type enzyme, pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000066
N-(bromobenzyl)-beta-D-gluco-1,5-deoxa-pyranosylamine
30°C, pH 5.0
0.628
N-(cyclohexyl)-beta-D-gluco-1,5-deoxa-pyranosylamine
30°C, pH 5.0
0.00022
N-(cyclohexylmethyl)-beta-D-gluco-1,5-deoxa-pyranosylamine
30°C, pH 5.0
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 55
-
20°C: about 55% of maximal activity, 55°C: about 40% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
beta-glucosidase genes from the transcriptome database of Stevia rebaudiana, transcriptome analysis. The enzyme expression pattern analyzed by real-time quantitative PCR shows no significant difference among different tissues, developmental stages, and cultivars under normal growth conditions, detailed overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
prediction of subcellular localization of SrRG1
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
the enzyme belongs to the glycoside hydrolase family 1, GH1
malfunction
agrobacterium-mediated transformation on instantaneous expression shows that overexpression of SrRG1 increases the accumulation of steviol content and decreases the major components and total SGs contents. SrRG1 may participate in the steviol glycosides catabolic pathway. However, the effect of silencing construct infiltration on steviol and SGs content is not significant and its expression pattern is constitutive, which most probably, attributed the hydrolysis of SGs to the secondary activity of SrRG1
metabolism
enzyme SrRG1 may participate in the steviol glycosides catabolic pathway. Total steviol glycosides content is the sum of rebaudioside A (RA), stevioside (St), rebaudioside C (RC), rebaudioside F (RF), and dulcoside A (DA)
additional information
beta-glucosidase genes from the transcriptome database of Stevia rebaudiana, transcriptome analysis. The enzyme expression pattern analyzed by real-time quantitative PCR shows no significant difference among different tissues, developmental stages, and cultivars under normal growth conditions
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RG1_RAUSE
540
0
60934
Swiss-Prot
other Location (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
61000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by the hanging-drop vapour diffusion technique at 20°C. Crystals reach a maximum dimension of about 0.2 * 0.15 * 0.05 mm, belong to space group I222 and diffract to 2.30 A resolution with unit-cell parameters of a = 102.8 A, b = 127.3 A and c = 215.8 A
-
enzyme in complex with the (1R,2S,3S,4R,5R)-4-(cyclohexylmethylamino)-5-(hydroxymethyl)cyclopentane-1,2,3-triol
wild type and mutant enzyme E186Q in complex with the substrate 1,2-(S)-dihydroraucaffricine and secologanin, hanging drop vapor diffusion method, using 0.01-0.3 M ammonium sulfate, 0.1 M sodium acetate, pH 4.5-5.0, 9-12% (w/v) PEG 4000 as precipitant buffer, and 20°C
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E420Q
-
the mutant shows 0.5% activity with raucaffricine compared to the wild type enzyme
E476A
-
the mutant shows 0.57% activity with raucaffricine compared to the wild type enzyme
E476L
-
the mutant shows 0.67% activity with raucaffricine compared to the wild type enzyme
F485Y
-
the mutant shows 24.24% activity with raucaffricine compared to the wild type enzyme
H193A
-
the mutant shows 43.66% activity with raucaffricine compared to the wild type enzyme
S390G
-
the mutant shows 30.91% activity with raucaffricine compared to the wild type enzyme
T189A
-
the mutant shows 63.94% activity with raucaffricine compared to the wild type enzyme
W392A
-
the mutant shows 1.21% activity with raucaffricine compared to the wild type enzyme
Y200A
-
the mutant shows 4.6% activity with raucaffricine compared to the wild type enzyme
additional information
SrRG1 overexpression and RNA interference (RNAi) silencing, transformation via Agrobacterium tumefaciens strain LBA4404 method
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic tree, expression pattern analysis by real-time quantitative PCR
for heterologous expression, RG cDNA cloned into the pSE280 vector. For optimum expression, RG cDNA cloned into the pQE-2 vector and expressed in Escherichia coli strain M15
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
the RG product vomilenine is a direct intermediate in ajmaline biosynthesis and utilization of raucaffricine for the ajmaline biosynthestic pathway could be a crucial and rate-limiting step in the formation of the antiarrythmic drug ajmaline
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schuebel, H.; Stoeckigt, J.; Feicht, R.; Simon, H.
Partial purification and characterization of raucaffricine beta-D-glucosidase from plant cell-suspension cultures of Rauwolfia serpentina Benth
Helv. Chim. Acta
69
538-547
1986
Rauvolfia caffra, Rauvolfia mannii, Rauvolfia serpentina, Rauvolfia verticillata
-
brenda
Warzecha, H.; Obitz, P.; Stockigt, J.
Purification, partial amino acid sequence and structure of the product of raucaffricine-O-beta-D-glucosidase from plant cell cultures of Rauwolfia serpentina
Phytochemistry
50
1099-1109
1999
Rauvolfia serpentina
brenda
Warzecha, H.; Gerasimenko, I.; Kutchan, T.M.; Stockigt, J.
Molecular cloning and functional bacterial expression of a plant glucosidase specifically involved in alkaloid biosynthesis
Phytochemistry
54
657-666
2000
Rauvolfia serpentina (Q9SPP9), Rauvolfia serpentina
brenda
Ruppert, M.; Panjikar, S.; Barleben, L.; Stckigt, J.
Heterologous expression, purification, crystallization and preliminary x-ray analysis of raucaffricine glucosidase, a plant enzyme specifically involved in Rauvolfia alkaloid biosynthesis
Acta Crystallogr. Sect. F
62
257-260
2006
Rauvolfia serpentina (Q9SPP9), Rauvolfia serpentina
brenda
Stoeckigt, J.; Panjikar, S.; Ruppert, M.; Barleben, L.; Ma, X.; Loris, E.; Hill, M.
The molecular architecture of major enzymes from ajmaline biosynthetic pathway
Phytochem. Rev.
6
15-34
2007
Rauvolfia serpentina
-
brenda
Xia, L.; Ruppert, M.; Wang, M.; Panjikar, S.; Lin, H.; Rajendran, C.; Barleben, L.; Stoeckigt, J.
Structures of alkaloid biosynthetic glucosidases decode substrate specificity
ACS Chem. Biol.
7
226-234
2012
Rauvolfia serpentina
brenda
Xia, L.; Rajendran, C.; Ruppert, M.; Panjikar, S.; Wang, M.; Stoeckigt, J.
High speed X-ray analysis of plant enzymes at room temperature
Phytochemistry
91
88-92
2013
Rauvolfia serpentina (Q9SPP9)
brenda
Xia, L.; Lin, H.; Staniek, A.; Panjikar, S.; Ruppert, M.; Hilgers, P.; Williardt, J.; Rajendran, C.; Wang, M.; Warzecha, H.; Jger, V.; Stckigt, J.
Ligand structures of synthetic deoxa-pyranosylamines with raucaffricine and strictosidine glucosidases provide structural insights into their binding and inhibitory behaviours
J. Enzyme Inhib. Med. Chem.
30
472-478
2015
Rauvolfia serpentina (Q9SPP9)
brenda
Yang, Y.; Hou, M.; Zhang, T.; Sun, Y.; Zhang, Y.; Huang, S.; Xu, X.; Yuan, H.
A beta-glucosidase gene from Stevia rebaudiana may be involved in the steviol glycosides catabolic pathway
Mol. Biol. Rep.
47
3577-3584
2020
Stevia rebaudiana (A0A7S5SML1)
brenda
EXTERNAL LINKS (specific for EC-Number 3.2.1.125)
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