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Information on EC 2.3.1.220 - 2,4,6-trihydroxybenzophenone synthase and Organism(s) Garcinia mangostana and UniProt Accession L7NCQ3

for references in articles please use BRENDA:EC2.3.1.220
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EC Tree
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).
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Select one or more organisms in this record: ?
This record set is specific for:
Garcinia mangostana
UNIPROT: L7NCQ3
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Word Map
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  • 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
The taxonomic range for the selected organisms is: Garcinia mangostana
The enzyme appears in selected viruses and cellular organisms
Synonyms
habps, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
benzophenone synthase
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
show the reaction diagram
additional information
?
-
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
-
-
?
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
3 malonyl-CoA + benzoyl-CoA
4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00965
benzoyl-CoA
pH 7.0, 30°C
0.0164
malonyl-CoA
pH 7.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0495
benzoyl-CoA
pH 7.0, 30°C
0.0582
malonyl-CoA
pH 7.0, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.14
benzoyl-CoA
pH 7.0, 30°C
3.55
malonyl-CoA
pH 7.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.97
sequence calculation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
phylogenetic tree
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TBSYN_GARMA
391
0
42712
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42700
xx * 42700, about, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
xx * 42700, about, sequence calculation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amin acid sequence determination and analysis, sequence comparison and phylogenetic tree
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team