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5.3.2.1: phenylpyruvate tautomerase

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

Word Map on EC 5.3.2.1

Reaction

keto-phenylpyruvate
=
enol-phenylpyruvate

Synonyms

CaaD, CCH2, cis-3-chloroacrylic acid dehalogenase, cis-CaaD, Macrophage migration inhibitory factor, macrophage migration inhibitory factor tautomerase, MIF, MIF tautomerase, phenyl(enol)pyruvate tautomerase, Phenylpyruvate keto-enol tautomerase, Phenylpyruvic keto-enol isomerase, PPT, Tautomerase, phenylpyruvate, trans-3-chloroacrylic acid dehalogenase

ECTree

     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.2 Interconverting keto- and enol-groups
                5.3.2.1 phenylpyruvate tautomerase

Engineering

Engineering on EC 5.3.2.1 - phenylpyruvate tautomerase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P1(A)M2
insertion abolishes activity
P1G
mutation substantially reduces the catalytic activity
E16A
kinetics similar to wild-type
K32A
-
15fold decrease in Ki-value for the competitive inhibitor, (E)-2-fluoro-p-hydroxycinnamate compared to wild-type enzyme, turnover number for enol-phenylpyruvate is 9% of that for the wild-type enzyme, turnover number for enol-(p-hydroxyphenyl)pyruvate is 11% of that for the wild-type enzyme, the ratio of turnover number and Km-value for enol-phenylpyruvate is 8% of that for the wild-type enzyme, the ratio of turnover number and KM-value for enol(p-hydroxyphenyl)pyruvate is 16% of the value for the wild-type enzyme
K32R
-
modest decrease in the stereoselectivity of the reaction and in the binding affinity of the competitive inhibitor, (E)-2-fluoro-p-hydroxycinnamate, turnover number for enol-phenylpyruvate is 47% of that for the wild-type enzyme, turnover number for enol-(p-hydroxyphenyl)pyruvate is 110% of that for the wild-type enzyme, the ratio of turnover number and Km-value for enol-phenylpyruvate or enol(p-hydroxyphenyl)pyruvate is about 70% of the value for the wild-type enzyme
N97A
the ratio of turnover number to Km-value for enol-phenylpyruvate is 21.3fold higher than that of the wild-type enzyme, the ratio of turnover number to Km-value for enol-(p-hydroxyphenyl)pyruvate is 1.5fold lower than that of the wild-type enzyme, 5fold increase in Ki-value for (E)-2-fluoro-p-hydroxycinnamate compared to the wild-type enzyme
P1A
the ratio of turnover number to Km-value for enol-phenylpyruvate is 232fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value for enol-(p-hydroxyphenyl)pyruvate is 114fold lower than that of the wild-type enzyme
P1F
-
mutant enzyme is completely inactive
P1G
the ratio of turnover number to Km-value for enol-phenylpyruvate is 232fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value for enol-(p-hydroxyphenyl)pyruvate is 143fold lower than that of the wild-type enzyme
P1S
-
mutant enzyme is nearly inactive
Y95F
the ratio of turnover number to Km-value for enol-phenylpyruvate is 1.3fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value for enol-(p-hydroxyphenyl)pyruvate is 1.5fold higher than that of the wild-type enzyme
E52Q
-
mutation in alpha-subunit, 1.6fold increase in ratio of kcat to Km value
P1A
-
mutation in beta-subunit, 8fold decrease in ratio of kcat to Km value
R11A
-
mutation in alpha-subunit, 15fold decrease in ratio of kcat to Km value
R8A
-
mutation in alpha-subunit, 19fold decrease in ratio of kcat to Km value
E52Q
-
mutation in alpha-subunit, 1.6fold increase in ratio of kcat to Km value
-
P1A
-
mutation in beta-subunit, 8fold decrease in ratio of kcat to Km value
-
R11A
-
mutation in alpha-subunit, 15fold decrease in ratio of kcat to Km value
-
R8A
-
mutation in alpha-subunit, 19fold decrease in ratio of kcat to Km value
-
additional information
-
modification of Pro1, e.g. via isothiocyanate inhibitors, alters the tertiary, but not the secondary or quaternary, structure of the trimer without affecting its thermodynamic stability, overview