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Information on EC 4.3.3.2 - strictosidine synthase and Organism(s) Rauvolfia serpentina and UniProt Accession P68175
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4.3.3.2 strictosidine synthaseIUBMB Comments
Catalyses a Pictet-Spengler reaction between the aldehyde group of secologanin and the amino group of tryptamine [4,5]. Involved in the biosynthesis of the monoterpenoid indole alkaloids.
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Word Map
- 4.3.3.2
- indole
- roseus
- catharanthus
-
terpenoid
-
monoterpenoid
- rauvolfia
- vindoline
- periwinkle
- serpentina
-
pictet-spengler
- synthesis
- ajmalicine
-
catharanthine
-
six-bladed
- tabersonine
- medicine
-
ophiorrhiza
-
elicitor-responsive
- pumila
- orca
- drug development
- biotechnology
- pharmacology
The taxonomic range for the selected organisms is: Rauvolfia serpentina
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
strictosidine synthase, ojstr, osstrl2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-alpha(S)-strictosidine + H2O = tryptamine + secologanin
catalytic reaction mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
Pictet-Spengler condensation between tryptamine and secologanin
condensation
-
Pictet-Spengler condensation between tryptamine and secologanin
condensation of aldehyde function with amine function
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
3-alpha(S)-strictosidine tryptamine-lyase (secologanin-forming)
Catalyses a Pictet-Spengler reaction between the aldehyde group of secologanin and the amino group of tryptamine [4,5]. Involved in the biosynthesis of the monoterpenoid indole alkaloids.
CAS REGISTRY NUMBER
COMMENTARY
69669-72-3
-
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
3-[(tert-butoxycarbonyl)amino]propyl (2S,3R,4S)-3-ethenyl-2-(beta-D-glucopyranosyloxy)-4-(2-oxoethyl)-3,4-dihydro-2H-pyran-5-carboxylate + secologanin
? + H2O
competitive to strictosidine
-
-
?
5-fluorotryptamine + secologanin
5-fluoro-3-alpha(S)-strictosidine + H2O
-
-
-
?
6-fluorotryptamine + secologanin
6-fluoro-3-alpha(S)-strictosidine + H2O
-
-
-
?
6-methoxyltryptamine + secologanin
6-methoxy-3-alpha(S)-strictosidine + H2O
-
-
-
?
6-methyltryptamine + secologanin
6-methyl-3-alpha(S)-strictosidine + H2O
-
-
-
?
7-azatryptamine + secologanin
3-alpha(S)-12-azastrictosidine
assay at pH 7.0, 28°C, reaction stopped by adding methanol
-
-
?
7-methyltryptamine + secologanin
7-methyl-3-alpha(S)-strictosidine + H2O
-
-
-
?
but-3-yn-1-yl (2S,3R,4S)-3-ethenyl-2-(beta-D-glucopyranosyloxy)-4-(2-oxoethyl)-3,4-dihydro-2H-pyran-5-carboxylate + secologanin
? + H2O
competitive to strictosidine
-
-
?
methyl (2R,4S)-2-(2-methylpropoxy)-4-(2-oxoethyl)-3,4-dihydro-2H-pyran-5-carboxylate + tryptamine
methyl (2R,4S)-2-(2-methylpropoxy)-4-[(1S)-2,3,4,9-tetrahydro-1H-beta-carbolin-1-ylmethyl]-3,4-dihydro-2H-pyran-5-carboxylate + H2O
cis- and trans-isomers are equally well accepted as substrates
-
-
?
methyl (2R,4S)-2-(cyclohexyloxy)-4-(2-oxoethyl)-3,4-dihydro-2H-pyran-5-carboxylate + tryptamine
methyl (2R,4S)-2-(cyclohexyloxy)-4-[(1S)-2,3,4,9-tetrahydro-1H-beta-carbolin-1-ylmethyl]-3,4-dihydro-2H-pyran-5-carboxylate + H2O
significant preference for the trans-isomer
-
-
?
methyl (2R,4S)-2-ethoxy-4-(2-oxoethyl)-3,4-dihydro-2H-pyran-5-carboxylate + tryptamine
methyl (2R,4S)-2-ethoxy-4-[(1S)-2,3,4,9-tetrahydro-1H-beta-carbolin-1-ylmethyl]-3,4-dihydro-2H-pyran-5-carboxylate + H2O
cis- and trans-isomers are equally well accepted as substrates
-
-
?
methyl (2R,4S)-2-tert-butoxy-4-(2-oxoethyl)-3,4-dihydro-2H-pyran-5-carboxylate + tryptamine
methyl (2R,4S)-2-tert-butoxy-4-[(1S)-2,3,4,9-tetrahydro-1H-beta-carbolin-1-ylmethyl]-3,4-dihydro-2H-pyran-5-carboxylate + H2O
cis- and trans-isomers are equally well accepted as substrates
-
-
?
methyl (2S,4S)-2-(2-methylpropoxy)-4-(2-oxoethyl)-3,4-dihydro-2H-pyran-5-carboxylate + tryptamine
methyl (2S,4S)-2-(2-methylpropoxy)-4-[(1S)-2,3,4,9-tetrahydro-1H-beta-carbolin-1-ylmethyl]-3,4-dihydro-2H-pyran-5-carboxylate + H2O
cis- and trans-isomers are equally well accepted as substrates
-
-
?
methyl (2S,4S)-2-ethoxy-4-(2-oxoethyl)-3,4-dihydro-2H-pyran-5-carboxylate + tryptamine
methyl (2S,4S)-2-ethoxy-4-[(1S)-2,3,4,9-tetrahydro-1H-beta-carbolin-1-ylmethyl]-3,4-dihydro-2H-pyran-5-carboxylate + H2O
cis- and trans-isomers are equally well accepted as substrates
-
-
?
methyl (2S,4S)-2-tert-butoxy-4-(2-oxoethyl)-3,4-dihydro-2H-pyran-5-carboxylate + tryptamine
methyl (2S,4S)-2-tert-butoxy-4-[(1S)-2,3,4,9-tetrahydro-1H-beta-carbolin-1-ylmethyl]-3,4-dihydro-2H-pyran-5-carboxylate + H2O
cis- and trans-isomers are equally well accepted as substrates
-
-
?
prop-2-yn-1-yl (2S,3R,4S)-3-ethenyl-2-(beta-D-glucopyranosyloxy)-4-(2-oxoethyl)-3,4-dihydro-2H-pyran-5-carboxylate + secologanin
? + H2O
competitive to strictosidine
-
-
?
serotonin + secologanin
5-hydroxy-3-alpha(S)-strictosidine + H2O
-
-
-
?
tryptamine + secologanin
3-alpha(S)-strictosidine
the enzyme catalyses the biological Pictete-Spengler reaction of tryptamine and secologanin. Tryptamine is located at the bottom of the substrate binding pocket, where its primary amine group is connected with residue Glu309 by a hydrogen bond. The main amino acid residues involved in forming the active centre are Tyr105, Trp149, Val167, Met180, Val208, Phe226, Ser269, Met276, His277, His307, Phe308, Glu309, Leu323, and Phe324
-
-
?
tryptamine + secologanin
3-alpha(S)-strictosidine + H2O
the strictosidine synthase plays a central role in the biosynthesis of all structural types of monoterpenoid indole alkaloids, overview
-
-
?
tryptamine + secologanin
3-alpha(S)-strictosidine + H2O
assay at pH 7.0, 28°C, reaction stopped by adding methanol
-
-
?
tryptamine + secologanin
3-alpha(S)-strictosidine
-
involved in synthesis of monoterpenoid indole alkaloides
-
?
tryptamine + secologanin
3-alpha(S)-strictosidine
-
involved in synthesis of monoterpenoid indole alkaloides
-
?
tryptamine + secologanin
3-alpha(S)-strictosidine + H2O
-
the enzyme is as amine lyases and catalyzes a PictetSpengler-type condensation between tryptamine and the aldehyde secologanin which leads to the formation of (S)-strictosidine
-
-
?
additional information
?
-
substrate specificity, e.g. with tryptamine derivatives, overview. No activity with N-acetyl-5-hydroxytryptamine, N-methyltryptamine, N-omega-methyltryptamine, 2-methyl,5-hydroxytryptamine, 3-methylamine indole, 3-propylamine indole, 2-methyltryptamine, 2-ethyltryptamine, 5,7-dimethoxytryptamine, phenylalanine, histamine, dopamine, 5-methyltryptamine, 5-methoxytryptamine, 4,5-dimethyltryptamine, and 4-methyl-5-methoxytryptamine, and with secologanic acid, tarennoside, 18-n-butylsecologanin, and 18-tert-butylsecologanin, overview. Dihydrosecologanin and secologanin acid ethyl ester are poor substrates
-
-
?
additional information
?
-
-
substrate specificity, e.g. with tryptamine derivatives, overview. No activity with N-acetyl-5-hydroxytryptamine, N-methyltryptamine, N-omega-methyltryptamine, 2-methyl,5-hydroxytryptamine, 3-methylamine indole, 3-propylamine indole, 2-methyltryptamine, 2-ethyltryptamine, 5,7-dimethoxytryptamine, phenylalanine, histamine, dopamine, 5-methyltryptamine, 5-methoxytryptamine, 4,5-dimethyltryptamine, and 4-methyl-5-methoxytryptamine, and with secologanic acid, tarennoside, 18-n-butylsecologanin, and 18-tert-butylsecologanin, overview. Dihydrosecologanin and secologanin acid ethyl ester are poor substrates
-
-
?
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
tryptamine + secologanin
3-alpha(S)-strictosidine + H2O
the strictosidine synthase plays a central role in the biosynthesis of all structural types of monoterpenoid indole alkaloids, overview
-
-
?
tryptamine + secologanin
3-alpha(S)-strictosidine + H2O
-
the enzyme is as amine lyases and catalyzes a PictetSpengler-type condensation between tryptamine and the aldehyde secologanin which leads to the formation of (S)-strictosidine
-
-
?
tryptamine + secologanin
3-alpha(S)-strictosidine
-
involved in synthesis of monoterpenoid indole alkaloides
-
?
tryptamine + secologanin
3-alpha(S)-strictosidine
-
involved in synthesis of monoterpenoid indole alkaloides
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-dinitrofluorobenzene
5 mM, no inactivation after 30 min and 15% inactivation after 120 min in Tris-HCl, pH 8.0
4-(2-aminoethyl)-benzenesulfonyl fluoride
4 mM, 4% inactivation after 30 min and 12% inactivation after 120 min in 100 mM potassium phosphate buffer, pH 7.0
diethylpyrocarbonate
1 mM, 49% inactivation after 30 min and 63% inactivation after 120 min in 100 mM potassium phosphate, pH 6.0
N,N'-dicyclohexylcarbodiimide
0.05 mM, complete inactivation after 30 min in MES, pH 6.0
N-Acetylimidazole
10 mM, 5% inactivation after 30 min and 12% inactivation after 120 min in Tris-HCl, pH 8.0
N-ethyl-5-phenylisoxazolium-3'-sulfonate
1 mM leads to 48% inactivation after 30 min and 53% inactivation after 120 min in MES, pH 6.0, 5 mM leads to 80% inactivation after 30 min and 100% inactivation after 120 min in MES, pH 6.0
p-chlormercuribenzoate
1 mM, 34% inactivation after 30 min and 35% inactivation after 120 min in 100 mM potassium phosphate, pH 6.0
additional information
no inactivation by phenylmethanesulfonyl fluoride, L-chloro-3-(4-tosyl-amido)-4-phenyl-2-butanone and L-chloro-3-(4-tosyl-amido)-7-amino-2-heptanone after 30 and 120 min in 100 mM potassium phosphate buffer, pH 7.0
-
additional information
-
no inactivation by phenylmethanesulfonyl fluoride, L-chloro-3-(4-tosyl-amido)-4-phenyl-2-butanone and L-chloro-3-(4-tosyl-amido)-7-amino-2-heptanone after 30 and 120 min in 100 mM potassium phosphate buffer, pH 7.0
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
activities between 14.29 nKat/l and 67.15 nKat/l, depending on expression system, increased activity in presence of chaperone pG-Tf2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
involved in biosynthesis of monoterpenoid indole alkaloids
evolution
-
strictosidine synthases belong to the beta-propeller fold family characterized by an all-beta architecture with four to eight blades, each consisting of four antiparallel beta-sheets, arranged around a pseudo symmetry axis
physiological function
-
strictosidine synthases catalyze the formation of strictosidine, a key intermediate in the biosynthesis of a large variety of monoterpenoid indole alkaloids
additional information
-
the six bladed beta-propeller protein has two regions which cover the enzyme active site. The observed activity changes suggest important roles of both regions in protein folding, stability and catalysis
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). STSY_RAUSE
344
1
38162
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
values between 36000 and 41000, dependent on expression system
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the overall enzyme structure of STR1 represents a beta-propeller comprising 6 blades, which are radially arranged around a central 6fold pseudo-symmetry axis, containing three helices in the STR1 structure. Each propeller blade contains four beta-strands, which form a twisted, antiparallel beta-sheet, important role of covalently bound cysteine residues in the integrity of the substrate binding site and in the enzyme's overall structure, structure analysis, overview
additional information
-
the overall enzyme structure of STR1 represents a beta-propeller comprising 6 blades, which are radially arranged around a central 6fold pseudo-symmetry axis, containing three helices in the STR1 structure. Each propeller blade contains four beta-strands, which form a twisted, antiparallel beta-sheet, important role of covalently bound cysteine residues in the integrity of the substrate binding site and in the enzyme's overall structure, structure analysis, overview
additional information
-
the enzyme is a six bladed beta-propeller protein
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cocrystallized with inhibitor 6, the complete data are collected to 3.0 A resolution
crystals of free STR1 and co-crystallization of STR1 with each tryptamine and secologanin, crystal growing by hanging drop vapor diffusion, 302-304 K, 0.8 M potassium sodium tartrate tetrahydrate, pH 7.5 - 8.0, combined multiple wavelength anomalous dispersion and molecular replacement methods
2.95 A under cryoconditions, crystal growing by hanging drop vapor diffusion, 303 K, 0.8 M potassium sodium tartrate tetrahydrate,pH 7.5 - 8.0
-
crystals of free STR1 and co-crystallization of STR1 and tryptamine, 2.95 A and 2.38 A under cryoconditions, crystal growing by hanging drop vapor diffusion, 302-304 K, 0.8 M potassium sodium tartrate tetrahydrate, pH 7.5 - 8.0, multiple wavelength anomalous dispersion method
-
the crystal structure of STR1 in complex with strictosidine is solved at a resolution of 3.0 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
V208A
the mutant shows altered substrate specificity compared to the wild-type enzyme, e.g. increased activity with tryptamine, overview
V208A
-
Val208 plays a critical role in substrate recognition at the indole moiety of strictosidine
additional information
-
construction of a STR tandem gene sequence, that serves as template for the preparation of circular permutated STR variants is assembled in pET17b using a truncated version of the STR gene, the N-terminal 28 amino acid residues in STR which constitutes the native signal sequence, as well as the unstructured 11 amino acids at the C-terminus are deleted, leaving a 915-nucleotide truncated version of STR, several truncated variants all show reduced activity compared to the wild-type enzyme, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilized enzyme is more stable to changes in pH and temperature than soluble enzyme
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no loss of activity with 5% PEG, dimethylformamide, acetone, ethanol or DMSO
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column, Mono Q column, concentration to 10 mg/ml in 10 mM Tris-HCl pH 8.0 before crystallization
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned with His-tag, expression in Escherichia coli strain M15, after expression and Ni-NTA column removed by DAPase
expression in Escherichia coli, coexpression with chaerone pG-Tf2
cloned with His-tag, expression in Escherichia coli strain M15, after expression and Ni-NTA column removed by DAPase
-
expressed in Sf9 cells using the Bacullovirus system, enzyme is secreted into the medium
-
expression in Escherichia coli M15 cells, functional co-expression with strictosidine glucosidase
-
STR gene, expresssion of wild-type enzyme and mutant constructs in Escherichia coli strain BL21(DE3)pLysS
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
for modern industrial drug discovery, construction of alkaloid libraries with complex scaffolds and huge backbone diversity is of paramount importance. Strategies are reported that depend on single step strictosidine synthase-catalyzed reaction. Enzyme reengineering combined with chemical methodologies is straightforward to be accessed to produce a bunch of novel alkaloids with great scaffold diversity
synthesis
involved in the biosynthesis of almost all plant monoterpenoid indole alkaloids
medicine
synthesis
-
involved in the biosynthesis of almost all plant monoterpenoid indole alkaloids
medicine
-
anti-cancer, anti-hypertensive, anti-malaria and anti-arrhythmic ajmaline agents
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kutchan, T.M.; Bock, A.; Dittrich, H.
Heterologous expression of the plant proteins strictosidine synthase and berberine bridge enzyme in insect cell culture
Phytochemistry
35
353-360
1994
Rauvolfia serpentina
Hampp, N.; Zenk, M.H.
Homogeneous strictosidine synthase from cell suspension cultures of Rauvolfia serpentina
Phytochemistry
27
3811-3815
1988
Rauvolfia serpentina
-
Bracher, D.; Kutchan, T.M.
Strictosidine synthase from Rauvolfia serpentina: analysis of a gene involved in indole alkaloid biosynthesis
Arch. Biochem. Biophys.
294
717-723
1992
Rauvolfia mannii, Rauvolfia serpentina
Koepke, J.; Ma, X.; Fritzsch, G.; Michel, H.; Stockigt, J.
Crystallization and preliminary X-ray analysis of strictosidine synthase and its complex with the substrate tryptamine
Acta Crystallogr. Sect. D
61
690-693
2005
Rauvolfia serpentina
Ma, X.; Koepke, J.; Fritzsch, G.; Diem, R.; Kutchan, T.M.; Michel, H.; Stockigt, J.
Crystallization and preliminary X-ray crystallographic analysis of strictosidine synthase from Rauvolfia: the first member of a novel enzyme family
Biochim. Biophys. Acta
1702
121-124
2004
Rauvolfia serpentina
Ma, X.; Panjikar, S.; Koepke, J.; Loris, E.; Stockigt, J.
The Structure of Rauvolfia serpentina Strictosidine Synthase Is a Novel Six-Bladed {beta}-Propeller Fold in Plant Proteins
Plant Cell
18
907-920
2006
Rauvolfia serpentina (P68175), Rauvolfia serpentina
Loris, E.A.; Panjikar, S.; Ruppert, M.; Barleben, L.; Unger, M.; Schuebel, H.; Stoeckigt, J.
Structure-based engineering of strictosidine synthase: auxiliary for alkaloid libraries
Chem. Biol.
14
979-985
2007
Rauvolfia serpentina
Maresh, J.J.; Giddings, L.A.; Friedrich, A.; Loris, E.A.; Panjikar, S.; Trout, B.L.; Stoeckigt, J.; Peters, B.; OConnor, S.E.
Strictosidine synthase: mechanism of a Pictet-Spengler catalyzing enzyme
J. Am. Chem. Soc.
130
710-723
2008
Catharanthus roseus, Rauvolfia serpentina (P68175)
Stoeckigt, J.; Barleben, L.; Panjikar, S.; Loris, E.A.
3D-Structure and function of strictosidine synthase - the key enzyme of monoterpenoid indole alkaloid biosynthesis
Plant Physiol. Biochem.
46
340-355
2008
Catharanthus roseus (P18417), Rauvolfia serpentina (P68175), Rauvolfia serpentina
Yang, L.; Zou, H.; Zhu, H.; Ruppert, M.; Gong, J.; Stoeckigt, J.
Improved expression of His(6)-tagged strictosidine synthase cDNA for chemo-enzymatic alkaloid diversification
Chem. Biodivers.
7
860-870
2010
Rauvolfia serpentina (P68175)
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
Bernhardt, P.; OConnor, S.E.
Synthesis and biochemical evaluation of des-vinyl secologanin aglycones with alternate stereochemistry
Tetrahedron Lett.
50
7118-7120
2009
Rauvolfia serpentina (P68175)
Fischereder, E.; Pressnitz, D.; Kroutil, W.; Lutz, S.
Engineering strictosidine synthase: rational design of a small, focused circular permutation library of the beta-propeller fold enzyme
Bioorg. Med. Chem.
22
5633-5637
2014
Rauvolfia serpentina
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