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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

Reaction

5 malonyl-CoA =

1,3,6,8-Tetrahydroxynaphthalene
+ 5 CoA + 5 CO2 +
H2O

Synonyms

1,3,6,8-tetrahydroxynaphthalene synthase, PhlD, PKS, PKS III, PKS1, RppA, SCO1206, SoceCHS1, THN synthase, THNS, type III polyketide synthase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.233 1,3,6,8-tetrahydroxynaphthalene synthase

Engineering

Engineering on EC 2.3.1.233 - 1,3,6,8-tetrahydroxynaphthalene synthase

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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
C138A
-
inactive with malonyl-CoA
-
C138S
-
inactive with malonyl-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
C138A
-
the mutant loses the ability to decarboxylate malonyl-CoA
C138Q
-
the mutant loses the ability to decarboxylate malonyl-CoA
C138S
-
the mutation does not influence the decarboxylation of malonyl-CoA
F188A
-
inactive
F188S
-
inactive
F188Y
-
the mutant shows reduced catalytic efficiency with hexanoyl-CoA as substrate
H270A
-
inactive
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
N303D
-
inactive
N303H
-
inactive
N303Q
-
inactive
Y224F
-
the mutant is able to accept malonyl-CoA as a starter substrate
Y224G
-
the mutant shows reduced catalytic efficiency with hexanoyl-CoA as substrate
Y224L
Y224W
-
the mutant is able to accept malonyl-CoA as a starter substrate