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Information on EC 2.3.1.220 - 2,4,6-trihydroxybenzophenone synthase
for references in articles please use BRENDA:EC2.3.1.220
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.220 2,4,6-trihydroxybenzophenone synthase
IUBMB Comments
Involved in the biosynthesis of plant xanthones. The enzyme from the plant Hypericum androsaemum L can use 3-hydroxybenzoyl-CoA instead of benzoyl-CoA, but with lower activity (cf. EC 2.3.1.151, 2,3′,4,6-tetrahydroxybenzophenone synthase).
The enzyme appears in viruses and cellular organisms
- 2.3.1.220
- falciparum
- plasmodium
-
merozoite
- malaria
-
subunit-based
- erythrocyte
- aotus
-
high-activity
-
receptor-ligand
-
sporozoite
-
anti-malarial
-
multi-stage
-
protection-inducing
-
multiepitope
- hyaluronan
-
enzyme-treated
-
multi-antigenic
-
hyaluronan-binding
-
rhoptries
-
microneme
-
chemically-synthesized
-
rhoptry-associated
-
parasitophorous
showSynonyms
habps, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
benzophenone synthase
BPS
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 malonyl-CoA + benzoyl-CoA = 4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
-
-
-
-
3 malonyl-CoA + benzoyl-CoA = 4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
the enzyme catalyzes the iterative condensation of benzoyl-CoA with three molecules of malonyl-CoA to give a linear tetraketide intermediate, which is subsequently cyclized into 2,4,6-trihydroxybenzophenone via intramolecular Claisen condensation, catalytic mechanism, overview
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
hyperxanthone E biosynthesis, tetrahydroxyxanthone biosynthesis (from benzoate)
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SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:benzoyl-CoA malonyltransferase (2,4,6-trihydroxybenzophenone-forming)
Involved in the biosynthesis of plant xanthones. The enzyme from the plant Hypericum androsaemum L can use 3-hydroxybenzoyl-CoA instead of benzoyl-CoA, but with lower activity (cf. EC 2.3.1.151, 2,3',4,6-tetrahydroxybenzophenone synthase).
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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
3 malonyl-CoA + 3-hydroxybenzoyl-CoA
4 CoA + 2,3',4,6-tetrahydroxybenzophenone + 3 CO2
-
Substrates: 43.5% of the activity compared to benzoyl-CoA
Products: -
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?
3 malonyl-CoA + butyryl-CoA
4 CoA + 2,4,6-trihydroxybutyrophenone + 6-propyl-4-hydroxy-2-pyrone + 3 CO2
-
Substrates: formation of 36.8% 2,4,6-trihydroxybutyrophenone and 6-propyl-4-hydroxy-2-pyrone as side product
Products: -
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?
3 malonyl-CoA + hexanoyl-CoA
4 CoA + 4-hydroxy-6-pentyl-2H-pyran-2-one + 4-hydroxy-6-(2-oxoheptyl)-2H-pyran-2-one + 3 CO2
-
Substrates: -
Products: -
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?
3 malonyl-CoA + isobutyryl-CoA
4 CoA + 2,4,6-trihydroxyisobutyrophenone + 3 CO2
-
Substrates: formation of 46.4% 2,4,6-trihydroxyisobutyrophenone and 34.2% 6-isopropyl-4-hydroxy-2-pyrone as side product
Products: -
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?
3 malonyl-CoA + isobutyryl-CoA
4 CoA + phloroisobutyrophenone + 3 CO2
-
Substrates: -
Products: -
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?
3 malonyl-CoA + isovaleryl-CoA
4 CoA + phloroisovalerophenone + 3 CO2
-
Substrates: -
Products: -
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?
3 malonyl-CoA + phenylacetyl-CoA
4 CoA + 2,4,6-trihydroxyphenylbenzylketone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
2 malonyl-CoA + benzoyl-CoA
3 CoA + 6-phenyl-4-hydroxy-2-pyrone + 2 CO2
-
Substrates: reaction of mutant T135L, no activity with the wild-type enzyme. The T135L mutant adds only two acetyl groups to the benzoyl starter unit to form a triketide intermediate which then cyclized into 6-phenyl-4-hydroxy-2-pyrone via C5 keto-enol oxygen -> C1 lactonization
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?
2 malonyl-CoA + benzoyl-CoA
3 CoA + 6-phenyl-4-hydroxy-2-pyrone + 2 CO2
-
Substrates: reaction of mutant T135L, no activity with the wild-type enzyme. The T135L mutant adds only two acetyl groups to the benzoyl starter unit to form a triketide intermediate which then cyclized into 6-phenyl-4-hydroxy-2-pyrone via C5 keto-enol oxygen -> C1 lactonization
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?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
Substrates: -
Products: -
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?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
Substrates: a minor amount of tetraketide lactone and triketide lactone are also obtained
Products: -
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?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
Substrates: -
Products: -
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?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
-
Substrates: benzoyl-CoA is the preferred starter substrate of the wild-type enzyme, activity by wild-type enzyme and mutant T135L
Products: -
Products: -
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
-
Substrates: benzoyl-CoA is the preferred starter substrate of the wild-type enzyme, very low 2,4,6-trihydroxybenzophenone-forming activity with the mutant T135L
Products: -
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?
additional information
?
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Substrates: the recombinant enzyme produces 2,4,6-trihydroxybenzophenone as the predominant product with benzoyl CoA as substrate. It also accepts other substrates, such as other plant PKSs, and used 1-3 molecules of malonyl CoA to form various phloroglucinol-type and polyketide lactone-type compounds
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additional information
?
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Substrates: 3-hydroxybenzoyl-CoA is the second best starter substrate for the wild-type enzyme but a poor starter molecule for the mutant enzyme T135L, resulting in formation of 2,3',4,6-tetrahydroxybenzophenone, reaction of EC 2.3.1.151. Product identification by mass spectrometry. No activity by wild-type enzyme and mutant T135L with 2-hydroxybenzoyl-CoA, 4-hydroxybenzoyl-CoA, cinnamoyl-CoA, 2-coumaroyl-CoA, 3-coumaroyl-CoA, 4-coumaroyl-CoA, and acetyl-CoA
Products: -
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?
additional information
?
-
-
Substrates: the enzyme does not accept 2-hydroxybenzoyl-CoA and 4-hydroxybenzoyl-CoA, acetyl-CoA, and CoA esters of cinnamic acids
Products: -
Products: -
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additional information
?
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-
Substrates: chalcone synthase, CHS EC 2.3.1.74, shows broad substrate specificity, overview. Both aromatic and aliphatic CoA esters are accepted in the active site of the enzyme as a starter substrate for the complex condensation reaction. CHS converts benzoyl-CoA to phlorobenzophenone, i.e. 2,4,6-trihydroxybenzophenone, along with pyrone by-products, and it converts phenylacetyl-CoA to an unnatural aromatic polyketide, phlorobenzylketone, i.e. 2,4,6-trihydroxyphenylbenzylketone. Scutellaria baicalensis CHS also accepts aliphatic CoA esters, isovaleryl-CoA and isobutyryl-CoA, to produce phloroacylphenones. Hexanoyl-CoA only affords pyrone derivatives without formation of a new aromatic ring
Products: -
Products: -
?
additional information
?
-
-
Substrates: 3-hydroxybenzoyl-CoA is the second best starter substrate for the wild-type enzyme but a poor starter molecule for the mutant enzyme T135L, resulting in formation of 2,3',4,6-tetrahydroxybenzophenone, reaction of EC 2.3.1.151. The benzoyl-primed triketides are covalently attached to the catalytic Cys167. The wild-type enzyme catalyzes another acetyl addition to the intermediate triketide
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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
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
-
Substrates: -
Products: -
Products: -
?
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Conserved regions of the Plasmodium falciparum rhoptry-associated protein 3 mediate specific host-pathogen interactions during invasion of red blood cells.
Infections
Functional, Immunological and Three-Dimensional Analysis of Chemically Synthesised Sporozoite Peptides as Components of a Fully-Effective Antimalarial Vaccine.
Infections
Functional, immunological and three-dimensional analysis of chemically synthesised sporozoite peptides as components of a fully-effective antimalarial vaccine.
Latent Tuberculosis
Specific Binding Peptides from Rv3632: A Strategy for Blocking Mycobacterium tuberculosis Entry to Target Cells?
Latent Tuberculosis
Towards designing a synthetic antituberculosis vaccine: The Rv3587c peptide inhibits mycobacterial entry to host cells.
Lymphoma
Peptides derived from Mycobacterium tuberculosis Rv2301 protein are involved in invasion to human epithelial cells and macrophages.
Malaria
Atomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malaria.
Malaria
Biological and structural characteristics of the binding peptides from the sporozoite proteins essential for cell traversal (SPECT)-1 and -2.
Malaria
Conserved regions from Plasmodium falciparum MSP11 specifically interact with host cells and have a potential role during merozoite invasion of red blood cells.
Malaria
Emerging rules for subunit-based, multiantigenic, multistage chemically synthesized vaccines.
Malaria
Functional, Immunological and Three-Dimensional Analysis of Chemically Synthesised Sporozoite Peptides as Components of a Fully-Effective Antimalarial Vaccine.
Malaria
Functional, immunological and three-dimensional analysis of chemically synthesised sporozoite peptides as components of a fully-effective antimalarial vaccine.
Malaria, Falciparum
Biological and structural characteristics of the binding peptides from the sporozoite proteins essential for cell traversal (SPECT)-1 and -2.
Tuberculosis
Functional characterization of Mycobacterium tuberculosis Rv2969c membrane protein.
Tuberculosis
Mycobacterium tuberculosis Rv0679c protein sequences involved in host-cell infection: Potential TB vaccine candidate antigen.
Tuberculosis
Peptides derived from the Mycobacterium tuberculosis Rv1490 surface protein implicated in inhibition of epithelial cell entry: potential vaccine candidates?
Tuberculosis
Peptides from the Mycobacterium tuberculosis Rv1980c protein involved in human cell infection: insights into new synthetic subunit vaccine candidates.
Tuberculosis
The Mycobacterium tuberculosis membrane protein Rv0180c: Evaluation of peptide sequences implicated in mycobacterial invasion of two human cell lines.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
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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
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
malfunction
metabolism
additional information
evolution
-
biphenyl synthase and benzophenone synthase catalyze the formation of identical linear tetraketide intermediates from benzoyl-CoA and three molecules of malonyl-CoA but use alternative intramolecular cyclization reactions to form 3,5-dihydroxybiphenyl and 2,4,6-trihydroxybenzophenone, respectively, phylogenetic analysis, overview. The enzyme belongs to the type iIi polyketide synthase superfamily. The functionally diverse PKSs, which include BIS and BPS, and the ubiquitously distributed chalcone synthases form separate clusters, which originate from a gene duplication event prior to the speciation of the angiosperms
evolution
-
BPS is a type III polyketide synthase, PKS, and part of the chalcone synthase group of the superfamily of enzymes
evolution
crystal structures of biphenyl synthase from Malus domestica and benzophenone synthase from Hypericum androsaemum are compared with the structure of an archetypal type III polyketide synthase - chalcone synthase from Malus domestica. The results illuminate structural determinants of benzoic acid-specific type III PKSs and expand the understanding of the evolution of specialized metabolic pathways in plants
malfunction
-
the benzophenone synthaase is converted into a functional phenylpyrone synthase by the single amino acid substitution T135L in the initiation/elongation cavity, homology modeling. The intermediate triketide may be redirected into a smaller pocket in the active site cavity, resulting in phenylpyrone formation by lactonization
malfunction
-
the T135L mutant catalyzes the addition of only two acetyl groups to the benzoyl starter unit. The triketide is the final linear intermediate and cyclizes into phenylpyrone via C-5 keto-enol oxygen -> C-1 lactonization
metabolism
the enzyme catalyzes the formation of an intermediate, 2,4,6-trihydroxybenzophenone, in the biosynthetic pathway of alpha-mangostin
additional information
the catalytic triad is formed by Cys164, His303, and Asn336
additional information
-
residues involved in the initiation pocket are M217, I258, A260, and Y269, and in the elongation pocket T135, S136, T197, M199, T200, S219, M267, and G342, the catalytic triad is formed by residues C167, H307, and N340, molecular modeling constructed based on the crystal structure of Medicago sativa CHS2 complexed with resveratrol, PDB ID 1CGZ, overview
additional information
-
the catalytic triad is formed by Cys167, His307, aand Asn340
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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). TBSYN_GARMA
391
0
42712
Swiss-Prot
other Location (Reliability: 3)
TBSYN_HYPAN
395
0
42828
Swiss-Prot
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method using buffered protein solutions (10-15 mg/ml) mixed with equal volumes of the reservoir solution and incubated at 4°C. Crystal structures of biphenyl synthase from Malus domestica and benzophenone synthase from Hypericum androsaemum are compared with the structure of an archetypal type III polyketide synthase - chalcone synthase from Malus domestica
hanging-drop vapor-diffusion method, incubation at 4°C. Crystal structures of biphenyl synthase from Malusx02domestica and benzophenone synthase from Hypericum androsaemum are compared with the structure of an archetypal type III polyketide synthase: chalcone synthase from Malus domestica. Both biphenyl synthase and benzophenone synthase contain mutations that reshape their active-site cavities to prevent the binding of 4-coumaroyl-CoA and to favor the binding of small hydrophobic substrates. The active-site cavities of biphenyl synthase and benzophenone synthase also contain a novel pocket associated with their chain-elongation and cyclization reactions
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A257G
site-directed mutagenesis, altered substrate entrance in the active site structure compared to the wild-type enzyme. The mutant A257G gives similar enzyme products as the wild type with both benzoyl-CoA and 4-coumaroyl-CoA
G339S
site-directed mutagenesis, altered substrate entrance in the active site structure compared to the wild-type enzyme. The mutant G339S yields high amounts of both benzophenone and triketide lactone type with benzoyl-CoA but shows no activity for 4-coumaroyl-CoA
G339V
site-directed mutagenesis, altered substrate entrance in the active site structure compared to the wild-type enzyme. The mutant shows no activity with either benzoyl-CoA or 4-coumaroyl-CoA
T133L
site-directed mutagenesis, altered substrate entrance in the active site structure compared to the wild-type enzyme. With benzoyl-CoA as a starter, the T133L mutant yields triketide lactone as the major enzymatic product
T135L
-
the T135L mutant catalyzes the addition of only two acetyl groups to the benzoyl starter unit. The triketide is the final linear intermediate and cyclizes into phenylpyrone via C-5 keto-enol oxygen -> C-1 lactonization. The T135L substitution opens a new pocket, the entrance of which is blocked in the wild-type enzyme by hydrogen bond formation between the threonine side chain and the backbone. Because of the interaction of the lipophilic side chain of the introduced leucine residue with the phenyl group of the growing polyketide chain, the triketide in the active site cavity of the T135L mutant may be redirected into the new pocket
T135F
-
site-directed mutagenesis, the mutant functionally resembles the wild-type enzyme
T135L
-
site-directed mutagenesis, the benzophenone synthaase is converted into a functional phenylpyrone synthase by the single amino acid substitution in the initiation/elongation cavity, chalcone synthase-based homology modeling, overview. The intermediate triketide may be redirected into a smaller pocket in the active site cavity, resulting in phenylpyrone formation by lactonization. Compared with the initiation/elongation cavity of BPS, the size of the newly accessible pocket in PPS is smaller and does not allow for a third acetyl addition to the growing polyketide chain, resulting in the release of the intermediate triketide as 6-phenyl-4-hydroxy-2-pyrone
T135S
-
site-directed mutagenesis, the mutant functionally resembles the wild-type enzyme
additional information
homology model of wild-type GmBPS and GmBPS mutants A257G, T133L, G339V, and G339S, active-site architectures by surface models and substrate entrances, overview
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
reccombinant N-terminally His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amin acid sequence determination and analysis, sequence comparison and phylogenetic tree
expression of N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after treatment with yeast extract benzophenone synthase activity in shoot cultures continues to rise after elicitation and peaks at 18 h
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schmidt, W.; Beerhues, L.
Alternative pathways of xanthone biosynthesis in cell cultures of Hypericum androsaemum
FEBS Lett.
420
143-146
1997
Hypericum androsaemum
brenda
Morita, H.; Takahashi, Y.; Noguchi, H.; Abe, I.
Enzymatic Formation of Unnatural Aromatic Polyketides by Chalcone Synthase
Biochem. Biophys. Res. Commun.
279
190-195
2000
Scutellaria baicalensis
brenda
Klundt, T.; Bocola, M.; Luetge, M.; Beuerle, T.; Liu, B.; Beerhues, L.
A single amino acid substitution converts benzophenone synthase into phenylpyrone synthase
J. Biol. Chem.
284
30957-30964
2009
Hypericum androsaemum
brenda
Beerhues, L.; Liu, B.
Biosynthesis of biphenyls and benzophenones-evolution of benzoic acid-specific type III polyketide synthases in plants
Phytochemistry
70
1719-1727
2009
Sorbus aucuparia
brenda
Nualkaew, N.; Morita, H.; Shimokawa, Y.; Kinjo, K.; Kushiro, T.; De-Eknamkul, W.; Ebizuka, Y.; Abe, I.
Benzophenone synthase from Garcinia mangostana L. pericarps
Phytochemistry
77
60-69
2012
Garcinia mangostana (L7NCQ3)
brenda
Stewart, C.; Woods, K.; Macias, G.; Allan, A.C.; Hellens, R.P.; Noel, J.P.
Molecular architectures of benzoic acid-specific type III polyketide synthases
Acta Crystallogr. Sect. D
73
1007-1019
2017
Hypericum androsaemum (Q8SAS8)
brenda
Belkheir, A.K.; Gaid, M.; Liu, B.; Haensch, R.; Beerhues, L.
Benzophenone synthase and chalcone synthase accumulate in the mesophyll of Hypericum perforatum leaves at different developmental stages
Front. Plant Sci.
7
921
2016
Hypericum perforatum
brenda
Tocci, N.; Gaid, M.; Kaftan, F.; Belkheir, A.K.; Belhadj, I.; Liu, B.; Svatos, A.; Haensch, R.; Pasqua, G.; Beerhues, L.
Exodermis and endodermis are the sites of xanthone biosynthesis in Hypericum perforatum roots
New Phytol.
217
1099-1112
2018
Hypericum perforatum
brenda
Moon, U.R.; Mitra, A.
A mechanistic insight into hydrogen peroxide-mediated elicitation of bioactive xanthones in Hoppea fastigiata shoot cultures
Planta
244
259-274
2016
Hoppea fastigiata
brenda
EXTERNAL LINKS (specific for EC-Number 2.3.1.220)
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Release 2023.1 (January 2023)
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