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Information on EC 2.3.1.233 - 1,3,6,8-tetrahydroxynaphthalene synthase and Organism(s) Streptomyces coelicolor and UniProt Accession Q9FCA7

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EC Tree
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.
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This record set is specific for:
Streptomyces coelicolor
UNIPROT: Q9FCA7
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The taxonomic range for the selected organisms is: Streptomyces coelicolor
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
1,3,6,8-tetrahydroxynaphthalene synthase, pks iii, sco1206, thn synthase, socechs1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,3,6,8-tetrahydroxynaphthalene synthase
-
type III polyketide synthase
-
1,3,6,8-tetrahydroxynaphthalene synthase
-
-
PKS1
-
-
-
-
SCO1206
-
-
-
-
THN synthase
-
-
type III polyketide synthase
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
show the reaction diagram
-
-
-
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
show the reaction diagram
-
-
-
-
?
acetoacetyl-CoA + 2 malonyl-CoA
4-hydroxy-6-methyl-2-pyrone + CoA + CO2 + H2O
show the reaction diagram
-
-
-
-
?
acetyl-CoA + 2 malonyl-CoA
? + CoA + CO2 + H2O
show the reaction diagram
-
-
-
-
?
benzoyl-CoA + 2 malonyl-CoA
4-hydroxy-6-phenyl-2H-pyran-2-one + CoA + CO2 + H2O
show the reaction diagram
-
-
-
-
?
hexanoyl-CoA + 2 malonyl-CoA
4-hydroxy-6-pentyl-2H-pyran-2-one + CoA + CO2 + H2O
show the reaction diagram
-
-
-
-
?
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
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
show the reaction diagram
-
-
-
?
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00358
malonyl-CoA
at pH 7.5 and 22°C
0.0014 - 0.0234
malonyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008
malonyl-CoA
at pH 7.5 and 22°C
0.002 - 79.2
malonyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.133 - 5.74
malonyl-CoA
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
x * 43000, SDS-PAGE
43000
-
x * 43000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 43000, SDS-PAGE
?
-
x * 43000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C106S
-
inactive
C138A
-
inactive with malonyl-CoA
C138S
-
inactive with malonyl-CoA
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-affinity column chromatography
nickel-nitrilotriacetic acid-agarose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli BL21(DE3) cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team