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Information on EC 2.3.1.233 - 1,3,6,8-tetrahydroxynaphthalene synthase
for references in articles please use BRENDA:EC2.3.1.233
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.233 1,3,6,8-tetrahydroxynaphthalene synthase
IUBMB Comments
Isolated from the fungus Colletotrichum lagenarium , and the bacteria Streptomyces coelicolor [2,3] and Streptomyces peucetius . It only uses malonyl-CoA, without invovement of acetyl-CoA.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 2.3.1.233
- polyketide
- coelicolor
- flaviolin
- synthases
-
streptomycete
- venezuelae
- accase
- griseus
-
starter
- chalcone
- synthesis
showSynonyms
1,3,6,8-tetrahydroxynaphthalene synthase, pks iii, sco1206, thn synthase, socechs1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,3,6,8-tetrahydroxynaphthalene synthase
PhlD
PKS
PKS III
PKS1
RppA
SCO1206
THN synthase
THNS
type III polyketide synthase
PKS1
-
-
-
-
RppA
-
-
-
-
SCO1206
-
-
-
-
THNS
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5 malonyl-CoA = 1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
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PATHWAY SOURCE
PATHWAYS
MetaCyc
flaviolin dimer and mompain biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA C-acyl transferase (1,3,6,8-tetrahydroxynaphthalene forming)
Isolated from the fungus Colletotrichum lagenarium [1], and the bacteria Streptomyces coelicolor [2,3] and Streptomyces peucetius [4]. It only uses malonyl-CoA, without invovement of acetyl-CoA.
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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
acetoacetyl-CoA + methylmalonyl-CoA
3,6-dimethyl-4-hydroxy-2-pyrone + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
butyryl-CoA
4-hydroxy-6-propyl-2-pyrone + 4-hydroxy-6-(2'-oxopentyl)-2-pyrone + 1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
-
Substrates: 21% activity compared to acetoacetyl-CoA
Products: -
Products: -
?
hexanoyl-CoA
4-hydroxy-6-pentyl-2-pyrone + 4-hydroxy-6-(2'-oxoheptyl)-2-pyrone + CoA + CO2 + H2O
isobutyryl-CoA
4-hydroxy-6-isopropyl-2-pyrone + 4-hydroxy-6-(3'-methyl-2'-oxopropyl)-2-pyrone + CoA + CO2 + H2O
-
Substrates: 7% activity compared to acetoacetyl-CoA
Products: -
Products: -
?
isovaleryl-CoA
4-hydroxy-6-isobutyl-2-pyrone + 4-hydroxy-6-(4'-methyl-2'-oxopentyl)-2-pyrone + CoA + CO2 + H2O
-
Substrates: 13% activity compared to acetoacetyl-CoA
Products: -
Products: -
?
lauroyl-CoA
1-(2,4,6-trihydroxyphenyl)-dodecan-1-one + 4-hydroxy-6-(2-oxotridecyl)-2H-pyran-2-one + CoA + CO2 + H2O
malonyl-CoA
5 1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA
6-heptyl-4-hydroxy-2-pyrone + 4-hydroxy-6-(2'-oxononyl)-2-pyrone + 4-hydroxy-6-(2',4',6'-trioxotridecyl)-2-pyrone + CoA + CO2 + H2O
-
Substrates: 6% activity compared to acetoacetyl-CoA
Products: -
Products: -
?
octanoyl-CoA + malonyl-CoA
4-hydroxy-6-(2',4',6'-trioxotridecyl)-2-pyrone + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
phenylacetyl-CoA
6-benzyl-4-hydroxy-2-pyrone + 4-hydroxy-6-(2'-oxo-3'-phenylpropyl)-2-pyrone + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
Substrates: -
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
Substrates: -
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
Substrates: -
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA
4-hydroxy-6-methyl-2-pyrone + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA
4-hydroxy-6-methyl-2-pyrone + CoA + CO2 + H2O
-
Substrates: 100% activity
Products: -
Products: -
?
acetoacetyl-CoA + 2 malonyl-CoA
4-hydroxy-6-methyl-2-pyrone + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + 2 malonyl-CoA
4-hydroxy-6-methyl-2-pyrone + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2 malonyl-CoA
? + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2 malonyl-CoA
? + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
benzoyl-CoA + 2 malonyl-CoA
4-hydroxy-6-phenyl-2H-pyran-2-one + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
benzoyl-CoA + 2 malonyl-CoA
4-hydroxy-6-phenyl-2H-pyran-2-one + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA
4-hydroxy-6-pentyl-2-pyrone + 4-hydroxy-6-(2'-oxoheptyl)-2-pyrone + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA
4-hydroxy-6-pentyl-2-pyrone + 4-hydroxy-6-(2'-oxoheptyl)-2-pyrone + CoA + CO2 + H2O
-
Substrates: 43% activity compared to acetoacetyl-CoA
Products: -
Products: -
?
hexanoyl-CoA + 2 malonyl-CoA
4-hydroxy-6-pentyl-2H-pyran-2-one + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + 2 malonyl-CoA
4-hydroxy-6-pentyl-2H-pyran-2-one + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
lauroyl-CoA
1-(2,4,6-trihydroxyphenyl)-dodecan-1-one + 4-hydroxy-6-(2-oxotridecyl)-2H-pyran-2-one + CoA + CO2 + H2O
Substrates: -
Products: -
Products: -
?
lauroyl-CoA
1-(2,4,6-trihydroxyphenyl)-dodecan-1-one + 4-hydroxy-6-(2-oxotridecyl)-2H-pyran-2-one + CoA + CO2 + H2O
Substrates: -
Products: -
Products: -
?
malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
Substrates: -
Products: -
Products: -
?
malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
Substrates: -
Products: -
Products: -
?
malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not use acetyl-CoA as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: less than 1% activity with acetyl-CoA, decanoyl-CoA, benzoyl-CoA, phenylacetyl-CoA, crotonoyl-CoA, and tiglyl-CoA
Products: -
Products: -
?
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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
malonyl-CoA
5 1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not use acetyl-CoA as substrate
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
Substrates: -
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
Substrates: -
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
Substrates: -
Products: -
Products: -
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
Substrates: -
Products: -
Products: -
?
malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
Substrates: -
Products: -
Products: -
?
malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
Substrates: -
Products: -
Products: -
?
malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0014
malonyl-CoA
-
mutant enzyme C184S, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C
0.0023
malonyl-CoA
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C
0.0085
malonyl-CoA
-
mutant enzyme C171S, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C
0.93
malonyl-CoA
-
in 100 mM Tris-HCl (pH 7.5), 1 mM EDTA, 1 mM 2-mercaptoethanol, at 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
malonyl-CoA
-
in 100 mM Tris-HCl (pH 7.5), 1 mM EDTA, 1 mM 2-mercaptoethanol, at 30°C
45.7
malonyl-CoA
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C
46.5
malonyl-CoA
-
mutant enzyme C171S, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C
79.2
malonyl-CoA
-
mutant enzyme C184S, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.55
malonyl-CoA
-
mutant enzyme C171S, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C
1.97
malonyl-CoA
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C
5.53
malonyl-CoA
-
mutant enzyme C184S, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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
metabolism
metabolism
-
the enzyme catalyses the synthesis of 1,3,6,8-tetrahydroxynaphthalene which is the key intermediate of melanin biosynthesis
metabolism
the enzyme catalyzes a major step in the biosynthetic pathway of phlorotannins (i.e., the synthesis of phloroglucinol monomers from malonyl-CoA)
metabolism
-
the enzyme catalyzes a major step in the biosynthetic pathway of phlorotannins (i.e., the synthesis of phloroglucinol monomers from malonyl-CoA)
-
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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). RPPA_STRC0
377
0
39081
Swiss-Prot
-
RPPA_STRCO
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
374
0
40934
Swiss-Prot
-
A0A841BJ88_9ACTN
348
0
37258
TrEMBL
-
A0A2S6R8F5_9PROT
355
0
38054
TrEMBL
-
A0A645H7T9_9ZZZZ
97
0
10412
TrEMBL
other Location (Reliability: 2)
A0A2S6U8G4_9PROT
348
0
36533
TrEMBL
-
A0A101RMZ6_9ACTN
394
0
42045
TrEMBL
-
A0A6J4J722_9ACTN
366
0
39712
TrEMBL
-
A0A399F763_9DEIN
354
0
37059
TrEMBL
-
A0A2S6TW46_9PROT
348
0
36787
TrEMBL
-
A0A2S6URD0_9PROT
347
0
38196
TrEMBL
-
A0A7W7LQV4_9ACTN
368
0
39971
TrEMBL
-
A0A2S6RA89_9PROT
251
0
26867
TrEMBL
-
A0A840QEE4_9PSEU
372
0
40390
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M Bicine, pH 8, and 18% (w/v) polyethylene glycol 6000, at 19°C
hanging drop vapor diffusion method, using 14% (w/v) PEG 8000, 200 mM MgCl2, 100 mM Na-MOPSO buffer (pH 7.0), 5 mM dithiothreitol, and 3% (w/v) sucrose
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C171S
-
the mutant shows about 4fold reduced catalytic efficiency compared to the wild type enzyme
C184S
-
the mutant shows about 2.5fold increased catalytic efficiency compared to the wild type enzyme
Y224A
-
the mutant shows 3% activity with malonyl-CoA compared to the wild type enzyme
Y224C
-
the mutant shows 50% activity with malonyl-CoA compared to the wild type enzyme
Y224F
-
the mutant shows 70% activity with malonyl-CoA compared to the wild type enzyme
Y224G
-
inactive with malonyl-CoA but capable of accepting acetoacetyl-CoA and acetyl-CoA
Y224H
-
inactive with malonyl-CoA but capable of accepting acetoacetyl-CoA and acetyl-CoA
Y224L
-
the mutant shows 65% activity with malonyl-CoA compared to the wild type enzyme
Y224M
-
the mutant shows 15% activity with malonyl-CoA compared to the wild type enzyme
Y224S
-
inactive with malonyl-CoA but capable of accepting acetoacetyl-CoA and acetyl-CoA
Y224A
-
the mutant shows 3% activity with malonyl-CoA compared to the wild type enzyme
-
Y224F
-
the mutant shows 70% activity with malonyl-CoA compared to the wild type enzyme
-
Y224S
-
inactive with malonyl-CoA but capable of accepting acetoacetyl-CoA and acetyl-CoA
-
A305I
-
the mutant produces only a triketide pyrone from hexanoyl-CoA as starter substrate
A305S
-
the mutant produces a triketide and tetraketide pyrone from hexanoyl-CoA as starter substrate
C138S
-
the mutation does not influence the decarboxylation of malonyl-CoA
F188Y
-
the mutant shows reduced catalytic efficiency with hexanoyl-CoA as substrate
H270N
-
the mutant produces triacetic acid lactone and flaviolin, an auto-oxidized product of 1,3,6,8-tetrahydroxynaphthalene, at a reduced rate
H270Q
-
the mutant retains high activity to catalyse polyketide formation, whereas the derailment products triacetic acid lactone and 6-acetonyl-4-hydroxy-2-pyrone (tetraketide lactone) are observed in increased amounts
Y224G
-
the mutant shows reduced catalytic efficiency with hexanoyl-CoA as substrate
Y224L
Y224L
-
the mutant shows increased catalytic efficiency with hexanoyl-CoA as substrate
Y224L
-
the mutant shows strongly reduced catalytic efficiency with malonyl-CoA compared to the wild type enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-nickel tetradentate column chromatography and Sephacryl-200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysS cells
heterologous expression of soceCHS1, bdsA, and bdsB from Sorangium cellulosum in Streptomyces coelicolor
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
heterologous expression of soceCHS1, bdsA, and bdsB from Sorangium cellulosum in Streptomyces coelicolor causes secretion of 1,8-dihydroxynaphthalene, a key precursor of dihydroxynaphthalene melanin, from Sorangium cellulosum
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Funa, N.; Ohnishi, Y.; Ebizuka, Y.; Horinouchi, S.
Alteration of reaction and substrate specificity of a bacterial type III polyketide synthase by site-directed mutagenesis
Biochem. J.
367
781-789
2002
Streptomyces griseus
brenda
Fujii, I.; Mori, Y.; Watanabe, A.; Kubo, Y.; Tsuji, G.; Ebizuka, Y.
Enzymatic synthesis of 1,3,6,8-tetrahydroxynaphthalene solely from malonyl coenzyme A by a fungal iterative type I polyketide synthase PKS1
Biochemistry
39
8853-8858
2000
Colletotrichum lagenaria
brenda
Maharjan, S.; Park, J.W.; Yoon, Y.J.; Lee, H.C.; Sohng, J.K.
Metabolic engineering of Streptomyces venezuelae for malonyl-CoA biosynthesis to enhance heterologous production of polyketides
Biotechnol. Lett.
32
277-282
2010
Streptomyces peucetius, Streptomyces peucetius ATCC 27952
brenda
Funa, N.; Ohnishi, Y.; Ebizuka, Y.; Horinouchi, S.
Properties and substrate specificity of RppA, a chalcone synthase-related polyketide synthase in Streptomyces griseus
J. Biol. Chem.
277
4628-4635
2002
Streptomyces griseus
brenda
Austin, M.B.; Izumikawa, M.; Bowman, M.E.; Udwary, D.W.; Ferrer, J.L.; Moore, B.S.; Noel, J.P.
Crystal structure of a bacterial type III polyketide synthase and enzymatic control of reactive polyketide intermediates
J. Biol. Chem.
279
45162-45174
2004
Streptomyces coelicolor
brenda
Li, S.; Grueschow, S.; Dordick, J.S.; Sherman, D.H.
Molecular analysis of the role of tyrosine 224 in the active site of Streptomyces coelicolor RppA, a bacterial type III polyketide synthase
J. Biol. Chem.
282
12765-12772
2007
Streptomyces coelicolor, Streptomyces coelicolor A3 (2), Streptomyces griseus
brenda
Izumikawa, M.; Shipley, P.R.; Hopke, J.N.; OHare, T.; Xiang, L.; Noel, J.P.; Moore, B.S.
Expression and characterization of the type III polyketide synthase 1,3,6,8-tetrahydroxynaphthalene synthase from Streptomyces coelicolor A3(2)
J. Ind. Microbiol. Biotechnol.
30
510-515
2003
Streptomyces coelicolor (Q9FCA7), Streptomyces coelicolor, Streptomyces coelicolor A3(2) (Q9FCA7), Streptomyces coelicolor A3(2)
brenda
Ghimire, G.P.; Oh, T.J.; Liou, K.; Sohng, J.K.
Identification of a cryptic type III polyketide synthase (1,3,6,8-tetrahydroxynaphthalene synthase) from Streptomyces peucetius ATCC 27952
Mol. Cells
26
362-367
2008
Streptomyces peucetius (B0FYK7), Streptomyces peucetius ATCC 27952 (B0FYK7)
brenda
Takano, Y.; Kubo, Y.; Shimizu, K.; Mise, K.; Okuno, T.; Furusawa, I.
Structural analysis of PKS1, a polyketide synthase gene involved in melanin biosynthesis in Colletotrichum lagenarium
Mol. Gen. Genet.
249
162-167
1995
Colletotrichum lagenaria
brenda
Cortes, J.; Velasco, J.; Foster, G.; Blackaby, A.P.; Rudd, B.A.; Wilkinson, B.
Identification and cloning of a type III polyketide synthase required for diffusible pigment biosynthesis in Saccharopolyspora erythraea
Mol. Microbiol.
44
1213-1224
2002
Saccharopolyspora erythraea, Saccharopolyspora erythraea E 8-7
brenda
Meslet-Cladiere, L.; Delage, L.; Leroux, C.J.; Goulitquer, S.; Leblanc, C.; Creis, E.; Gall, E.A.; Stiger-Pouvreau, V.; Czjzek, M.; Potin, P.
Structure/function analysis of a type III polyketide synthase in the brown alga Ectocarpus siliculosus reveals a biochemical pathway in phlorotannin monomer biosynthesis
Plant Cell
25
3089-3103
2013
Ectocarpus siliculosus (D8LJ35), Ectocarpus siliculosus, Ectocarpus siliculosus Ec 32 (D8LJ35)
brenda
Sone, Y.; Nakamura, S.; Sasaki, M.; Hasebe, F.; Kim, S.; Funa, N.
Identification and characterization of bacterial enzymes catalyzing the synthesis of 1,8-dihydroxynaphthalene, a key precursor of dihydroxynaphthalene melanin, from Sorangium cellulosum
Appl. Environ. Microbiol.
84
e00258-18
2018
Sorangium cellulosum
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