2.3.1.233: 1,3,6,8-tetrahydroxynaphthalene synthase
This is an abbreviated version!
For detailed information about 1,3,6,8-tetrahydroxynaphthalene synthase, go to the full flat file.
Word Map on EC 2.3.1.233
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2.3.1.233
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polyketide
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coelicolor
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flaviolin
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synthases
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streptomycete
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venezuelae
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accase
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griseus
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starter
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chalcone
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synthesis
- 2.3.1.233
- polyketide
- coelicolor
- flaviolin
- synthases
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streptomycete
- venezuelae
- accase
- griseus
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starter
- chalcone
- synthesis
Reaction
5 malonyl-CoA = + 5 CoA + 5 CO2 +
Synonyms
1,3,6,8-tetrahydroxynaphthalene synthase, PhlD, PKS, PKS III, PKS1, RppA, SCO1206, SoceCHS1, THN synthase, THNS, type III polyketide synthase
ECTree
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Engineering
Engineering on EC 2.3.1.233 - 1,3,6,8-tetrahydroxynaphthalene synthase
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C171S
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the mutant shows about 4fold reduced catalytic efficiency compared to the wild type enzyme
C184S
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the mutant shows about 2.5fold increased catalytic efficiency compared to the wild type enzyme
Y224A
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the mutant shows 3% activity with malonyl-CoA compared to the wild type enzyme
Y224C
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the mutant shows 50% activity with malonyl-CoA compared to the wild type enzyme
Y224F
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the mutant shows 70% activity with malonyl-CoA compared to the wild type enzyme
Y224G
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inactive with malonyl-CoA but capable of accepting acetoacetyl-CoA and acetyl-CoA
Y224H
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inactive with malonyl-CoA but capable of accepting acetoacetyl-CoA and acetyl-CoA
Y224L
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the mutant shows 65% activity with malonyl-CoA compared to the wild type enzyme
Y224M
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the mutant shows 15% activity with malonyl-CoA compared to the wild type enzyme
Y224S
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inactive with malonyl-CoA but capable of accepting acetoacetyl-CoA and acetyl-CoA
Y224A
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the mutant shows 3% activity with malonyl-CoA compared to the wild type enzyme
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Y224F
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the mutant shows 70% activity with malonyl-CoA compared to the wild type enzyme
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Y224S
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inactive with malonyl-CoA but capable of accepting acetoacetyl-CoA and acetyl-CoA
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A305I
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the mutant produces only a triketide pyrone from hexanoyl-CoA as starter substrate
A305S
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the mutant produces a triketide and tetraketide pyrone from hexanoyl-CoA as starter substrate
C138S
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the mutation does not influence the decarboxylation of malonyl-CoA
F188Y
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the mutant shows reduced catalytic efficiency with hexanoyl-CoA as substrate
H270N
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the mutant produces triacetic acid lactone and flaviolin, an auto-oxidized product of 1,3,6,8-tetrahydroxynaphthalene, at a reduced rate
H270Q
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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
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the mutant shows reduced catalytic efficiency with hexanoyl-CoA as substrate
Y224L
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the mutant shows increased catalytic efficiency with hexanoyl-CoA as substrate
Y224L
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the mutant shows strongly reduced catalytic efficiency with malonyl-CoA compared to the wild type enzyme