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2.2.1.9: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase

This is an abbreviated version!
For detailed information about 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase, go to the full flat file.

Word Map on EC 2.2.1.9

Reaction

isochorismate
+
2-oxoglutarate
=
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
 +
CO2

Synonyms

(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase, (1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxycyclohex-3-ene-1-carboxylate synthase, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic acid synthase, EC 2.5.1.64, EcMenD, MenD, Rv0555, SEPHCHC synthase, SHCHC synthase

ECTree

     2 Transferases
         2.2 Transferring aldehyde or ketonic groups
             2.2.1 Transketolases and transaldolases
                2.2.1.9 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase

Engineering

Engineering on EC 2.2.1.9 - 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F490A
0.6% of wild-type activity
I489A
1% of wild-type activity
K299A
150% of wild-type activity
L493A
80% of wild-type activity
R106A
mutation in the second subunit forming the active site, 10% of wild-type activity
R32A
mutation in the second subunit forming the active site, 30% of wild-type activity
R409A
3% of wild-type activity
R428A
1% of wild-type activity
E55D
-
about 30% decrease in catalytic efficiency
I148L
-
strong decrease in catalytic efficiency
K292Q
-
150% increase in catalytic efficiency
N117R/L478T
the mutant preferentially converts (5S,6S)-5,6-dihydroxycyclohexa-1,3-diene-1-carboxylate with a more than 70fold higher ratio than that for the wild type enzyme
Q118A
the mutant is completely inactive
R107I
the mutant uses (5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxylate as substrate with more than 6fold conversion compared to the wild type enzyme
R107K
-
no decrease in catalytic efficiency
R293K
-
slight increase in catalytic efficiency
R395A
the mutant shows a 160 and 1000fold decrease in kcat/Km value with respect to 2-oxoglutarate and isochorismate, respectively, compared to the wild type enzyme
R395K
R395K/R413K
the mutant shows a 6300 and 1300fold decrease in kcat/Km value with respect to 2-oxoglutarate and isochorismate, respectively, compared to the wild type enzyme
R413A
the mutant is completely inactive
R413K
S32A
-
slight decrease in catalytic efficiency
S391A
-
slight decrease in catalytic efficiency
R277A
-
the mutant has 18% of the wild type enzyme activity
R303A
-
the mutant has 56% of the wild type enzyme activity
R395K
-
4fold increase in Km value, 50% decrease in kcat value
R97A
-
the mutant has 50% of the wild type enzyme activity
S391A
-
minor effect on activity
S391Y
-
trace activity
R277A
-
the mutant has 18% of the wild type enzyme activity
-
R303A
-
the mutant has 56% of the wild type enzyme activity
-
R97A
-
the mutant has 50% of the wild type enzyme activity
-