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Information on EC 3.2.1.105 - 3alpha(S)-strictosidine beta-glucosidase and Organism(s) Rauvolfia serpentina and UniProt Accession Q8GU20

for references in articles please use BRENDA:EC3.2.1.105
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IUBMB Comments
Does not act on a number of closely related glycosides. Strictosidine is a precursor of indole alkaloids.
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This record set is specific for:
Rauvolfia serpentina
UNIPROT: Q8GU20
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The taxonomic range for the selected organisms is: Rauvolfia serpentina
The enzyme appears in selected viruses and cellular organisms
Synonyms
orca3, strictosidine glucosidase, strictosidine beta-d-glucosidase, strictosidine beta-glucosidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
strictosidine beta-D-glucosidase
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strictosidine beta-glucosidase
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strictosidine glucosidase
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glucosidase, strictosidine beta-
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-
-
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SGD
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-
-
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strictosidine beta-D-glucohydrolase
-
-
-
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strictosidine beta-D-glucosidase
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-
-
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strictosidine beta-glucosidase
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-
-
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strictosidine glucosidase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
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SYSTEMATIC NAME
IUBMB Comments
strictosidine beta-D-glucohydrolase
Does not act on a number of closely related glycosides. Strictosidine is a precursor of indole alkaloids.
CAS REGISTRY NUMBER
COMMENTARY hide
73379-57-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
18,19-dihydrostrictosidine + H2O
D-glucose + 18,19-dihydrostrictosidine aglycone
show the reaction diagram
-
-
-
?
5alpha-carboxystrictosidine + H2O
D-glucose + 5alpha-carboxystrictosidine aglycone
show the reaction diagram
-
-
-
?
dolichantoside + H2O
D-glucose + dolichantoside aglycone
show the reaction diagram
-
-
-
?
Nbeta-acetylstrictosidine + H2O
D-glucose + Nbeta-acetylstrictosidine aglycone
show the reaction diagram
weak substrate
-
-
?
Nbeta-methylstrictosidine + H2O
D-glucose + Nbeta-methylstrictosidine aglycone
show the reaction diagram
weak substrate
-
-
?
strictosidine + H2O
D-glucose + strictosidine aglycone
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
strictosidine + H2O
D-glucose + strictosidine aglycone
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
8.8% inhibition at 1 mM
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-(cyclohexylmethyl)-beta-D-gluco-1,5-deoxa-pyranosylamine
the inhibitor anchors exclusively in the catalytic active site by competition with appropriate enzyme substrates
serpentine
25.2% inhibition at 1 mM
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
strictosidine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.127
N-(bromobenzyl)-beta-D-gluco-1,5-deoxa-pyranosylamine
30°C, pH 5.0
6.7
N-(cyclohexylmethyl)-beta-D-gluco-1,5-deoxa-pyranosylamine
30°C, pH 5.0
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2 - 8
50% of maximal activity at oH 4.2, above pH 5.2 the activity slowly decreases up to pH 8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
epidermis of aerial organs
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SG1_RAUSE
532
0
60881
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
450000
gel filtration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with the N-(bromobenzyl)-beta-D-gluco-1,5-deoxa-pyranosylamine or N-(cyclohexylmethyl)-beta-D-gluco-1,5-deoxa-pyranosylamine
2.48 A resolution, sitting- and hanging-drop vapour diffusion, 0.3 M ammonium sulfate, 0.1 M sodium acetate, pH 4.6, 10% PEG 4000
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column, dipeptidyl aminopeptidase, Mono Q column
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
fusion protein with intein tag, expressed in Escherichia coli
heterologously expressed in Escherichia coli
expression in Escherichia coli M15 cells, functional co-expression with strictosidine synthase
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expression in Escherichia coli strain Top 10 with His-tag
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functional co-expression in Escherichia coli strain M15 with strictosidine synthase, EC 4.3.3.2, resulting in cathenamine formation from administered tryptamine and secologanin
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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plays central role in indole alkaloid biosynthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gerasimenko, I.; Sheludko, Y.; Ma, X.; Stockigt, J.
Heterologous expression of a Rauvolfia cDNA encoding strictosidine glucosidase, a biosynthetic key to over 2000 monoterpenoid indole alkaloids
Eur. J. Biochem.
269
2204-2213
2002
Rauvolfia serpentina (Q8GU20), Rauvolfia serpentina
Manually annotated by BRENDA team
Barleben, L.; Ma, X.; Koepke, J.; Peng, G.; Michel, H.; Stoeckigt, J.
Expression, purification, crystallization and preliminary X-ray analysis of strictosidine glucosidase, an enzyme initiating biosynthetic pathways to a unique diversity of indole alkaloid skeletons
Biochim. Biophys. Acta
1747
89-92
2005
Rauvolfia serpentina
Manually annotated by BRENDA team
Stockigt, J.; Hammes, B.; Ruppert, M.
Construction and expression of a dual vector for chemo-enzymatic synthesis of plant indole alkaloids in Escherichia coli
Nat. Prod. Res.
24
759-766
2010
Rauvolfia serpentina
Manually annotated by BRENDA team
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 (Q8GU20)
Manually annotated by BRENDA team
Guirimand, G.; Courdavault, V.; Lanoue, A.; Mahroug, S.; Guihur, A.; Blanc, N.; Giglioli-Guivarch, N.; St-Pierre, B.; Burlat, V.
Strictosidine activation in Apocynaceae: Towards a nuclear time bomb?
BMC Plant Biol.
10
182
2010
Catharanthus roseus (Q9M7N7), Catharanthus roseus, Rauvolfia serpentina (Q8GU20), Rauvolfia serpentina
Manually annotated by BRENDA team
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 (Q8GU20)
Manually annotated by BRENDA team