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2.3.1.253: phloroglucinol synthase

This is an abbreviated version!
For detailed information about phloroglucinol synthase, go to the full flat file.

Reaction

3 malonyl-CoA =

phloroglucinol
+ 3 CO2 + 3 CoA

Synonyms

PhlD, phloroglucinol synthase, type III polyketide synthase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.253 phloroglucinol synthase

Engineering

Engineering on EC 2.3.1.253 - phloroglucinol synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A181S
-
the mutant shows 110% of wild type specific activity
A289R
the mutant shows 1.4fold improved catalytic efficiency compared to the wild type enzyme
A60L
the mutant still retains the wild type activity to react with lauroyl-CoA
A82T
-
the mutant shows wild type specific activity
H24L
the mutant shows reduced reactivity toward lauroyl-CoA and has lost the ability to produce phloroglucinol
H24V
the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
K210L
the mutant shows 1.9fold improved catalytic efficiency compared to the wild type enzyme
K210L/Y256R
the mutant shows 0.9fold improved catalytic efficiency compared to the wild type enzyme
L136M/S243T
-
the mutant shows 90% of wild type specific activity
L54V
-
the mutant shows 110% of wild type specific activity
L54V/A82T
-
the mutant shows wild type specific activity
L59M
the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
M21I
the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
M21T/L54V/A82T
-
the mutant shows 90% of wild type specific activity
M21T/L54V/A82T/A181S
-
the mutant shows wild type specific activity
M21T/L54V/A82T/S96R/A181S
-
the mutant shows 110% of wild type specific activity
M21T/N27D/A82T/A181S
-
the mutant shows 90% of wild type specific activity
M21T/N27D/L54V/A82T/A181S/S243T
-
the mutant shows wild type specific activity
M21T/N27D/L54V/A82T/L136M/A181S/S243T
-
the mutant shows 110% of wild type specific activity
N27D
-
the mutant shows 90% of wild type specific activity
S96R
-
the mutant shows 80% of wild type specific activity
Y256R
the mutant shows 1.9fold improved catalytic efficiency compared to the wild type enzyme
Y256R/A289R
the mutant shows 0.8fold improved catalytic efficiency compared to the wild type enzyme
A181S
-
the mutant shows 110% of wild type specific activity
-
A289R
-
the mutant shows 1.4fold improved catalytic efficiency compared to the wild type enzyme
-
A82T
-
the mutant shows wild type specific activity
-
H24L
-
the mutant shows reduced reactivity toward lauroyl-CoA and has lost the ability to produce phloroglucinol
-
H24V
-
the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
-
K210L
-
the mutant shows 1.9fold improved catalytic efficiency compared to the wild type enzyme
-
K210L/Y256R
-
the mutant shows 0.9fold improved catalytic efficiency compared to the wild type enzyme
-
L136M/S243T
-
the mutant shows 90% of wild type specific activity
-
L54V
-
the mutant shows 110% of wild type specific activity
-
L59M
-
the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
-
M21I
-
the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
-
M21T
-
the mutant still retains the wild type activity to react with lauroyl-CoA
-
N27D
-
the mutant shows 90% of wild type specific activity
-
Y256R
-
the mutant shows 1.9fold improved catalytic efficiency compared to the wild type enzyme
-
Y256R/A289R
-
the mutant shows 0.8fold improved catalytic efficiency compared to the wild type enzyme
-