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Information on EC 3.2.1.125 - raucaffricine beta-glucosidase
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EC Tree
3.2.1.125 raucaffricine beta-glucosidaseIUBMB Comments
Highly specific; some other ajmalan glucoside alkaloids are hydrolysed, but more slowly.
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Word Map
- 3.2.1.125
- strictosidine
- serpentina
- rauvolfia
- indole
- ajmaline
-
monoterpenoid
-
glucosidases
- glycosides
-
deglucosylation
- hydrolases
- secologanin
- pharmacology
The enzyme appears in viruses and cellular organisms
Synonyms
raucaffricine-o-beta-d-glucosidase, raucaffricine glucosidase, raucaffricine beta-glucosidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glucosidase, raucaffricine beta-
-
-
-
-
raucaffricine beta-D-glucosidase
-
-
-
-
raucaffricine 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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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2,19,20-tetrahydroraucaffricine + H2O
17-O-acetylnorajmaline + D-glucose
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87% of activity compared to raucaffricine
-
-
?
1,2-(S)-dihydro-raucaffricine + H2O
2beta(R)-1,2-dihydrovomilenine + D-glucose
-
98% acivity compared to raucaffricine
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-
?
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
-
36% of activity compared to raucaffricine
-
-
?
1-methyl-1,2-dihydroraucaffricine + H2O
?
recombinant RG
-
?
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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95% of activity compared to raucaffricine
-
-
?
21-glucopyranosyl-hydroxysarpagan-17-al + H2O
?
recombinant RG
-
?
21-glucopyranosyl-hydroxysarpagan-17-ol + H2O
?
recombinant RG
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?
secologanin + H2O
secologanin aglycone
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0.24% acivity compared to raucaffricine
-
-
?
strictosidine + H2O
strictosidine aglycone + D-glucose
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1.18% acivity compared to raucaffricine
-
-
?
1,2-dihydroraucaffricine + H2O
2beta(R)-1,2-dihydrovomilenine + D-glucose
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-
-
-
?
1,2-dihydroraucaffricine + H2O
2beta(R)-1,2-dihydrovomilenine + D-glucose
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98% of activity compared to raucaffricine
-
-
?
raucaffricine + H2O
D-glucose + vomilenine
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-
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
best substrate, highly specific enzyme
-
?
raucaffricine + H2O
D-glucose + vomilenine
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involved in the biosynthesis of alkaloids, e.g. ajmaline
-
?
raucaffricine + H2O
D-glucose + vomilenine
specifically involved in alkaloid biosynthesis, e.g. ajmaline
vomilene is a direct intermediate in ajmaline biosynthesis
?
strictosidine + H2O
?
only recombinant RG, no substrate of native RG
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
raucaffricine + H2O
D-glucose + vomilenine
-
involved in the biosynthesis of alkaloids, e.g. ajmaline
-
?
raucaffricine + H2O
D-glucose + vomilenine
specifically involved in alkaloid biosynthesis, e.g. ajmaline
vomilene is a direct intermediate in ajmaline biosynthesis
?
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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
-
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
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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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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: 3)
A0A2G9H7Y3_9LAMI
413
0
47036
TrEMBL
other Location (Reliability: 3)
A0A2G9G609_9LAMI
555
0
62984
TrEMBL
other Location (Reliability: 2)
A0A2G9HA70_9LAMI
562
0
64057
TrEMBL
other Location (Reliability: 3)
A0A2G9GC87_9LAMI
556
0
62958
TrEMBL
other Location (Reliability: 3)
A0A2G9H2X6_9LAMI
564
0
64653
TrEMBL
other Location (Reliability: 3)
A0A2G9GGQ1_9LAMI
284
0
31967
TrEMBL
other Location (Reliability: 3)
A0A2G9HSZ3_9LAMI
563
0
64047
TrEMBL
other Location (Reliability: 3)
A0A2G9GGQ4_9LAMI
209
0
23969
TrEMBL
Mitochondrion (Reliability: 4)
A0A2G9HLG9_9LAMI
455
0
52211
TrEMBL
other Location (Reliability: 2)
A0A2G9GI54_9LAMI
508
0
57934
TrEMBL
other Location (Reliability: 5)
A0A2G9H821_9LAMI
565
0
64429
TrEMBL
other Location (Reliability: 3)
A0A2G9FXA6_9LAMI
546
0
62138
TrEMBL
other Location (Reliability: 2)
A0A2G9FZA9_9LAMI
556
0
63092
TrEMBL
other Location (Reliability: 3)
A0A2G9HNU4_9LAMI
543
0
62124
TrEMBL
other Location (Reliability: 2)
A0A2G9H7X7_9LAMI
661
0
74589
TrEMBL
other Location (Reliability: 2)
A0A2G9GQC8_9LAMI
535
0
61205
TrEMBL
other Location (Reliability: 3)
A0A2G9HKV4_9LAMI
613
0
70293
TrEMBL
other Location (Reliability: 2)
A0A2G9GB06_9LAMI
551
0
62911
TrEMBL
other Location (Reliability: 2)
A0A2G9HLV4_9LAMI
654
0
75120
TrEMBL
other Location (Reliability: 2)
A0A2G9GNC3_9LAMI
564
0
63752
TrEMBL
other Location (Reliability: 4)
A0A2G9GGZ4_9LAMI
551
0
63688
TrEMBL
other Location (Reliability: 2)
A0A2G9GGP3_9LAMI
562
0
63754
TrEMBL
other Location (Reliability: 3)
A0A2G9H7X5_9LAMI
564
0
64325
TrEMBL
other Location (Reliability: 3)
A0A2G9HA86_9LAMI
563
0
64099
TrEMBL
other Location (Reliability: 3)
A0A2G9HT66_9LAMI
565
0
64300
TrEMBL
other Location (Reliability: 3)
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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
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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
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.; Stöckigt, 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.; Jäger, V.; Stöckigt, 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
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