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
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5.3.2.1
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necrosis
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monocyte
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tnf
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endothelial
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lymphocyte
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chemokine
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autoimmune
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anti-mif
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glucocorticoid
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arthritis
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pulmonary
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artery
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leukocyte
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angiogenesis
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sepsis
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rheumatoid
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tnf-alpha
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lipopolysaccharide
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factor-alpha
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myocardial
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t-cells
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atherosclerosis
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chemotactic
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c-reactive
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pituitary
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chemoattractant
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infarct
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lupus
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lymphokine
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toll-like
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autocrine
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cxcr2
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synovial
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ifn-gamma
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il-1beta
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counter-regulator
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chemokine-like
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erythematosus
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immunoregulatory
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cell-mediated
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glomerulonephritis
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dehalogenation
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tautomerization
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counterregulates
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delayed-type
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pro-tumorigenic
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drug development
- 5.3.2.1
- necrosis
- monocyte
- tnf
- endothelial
- lymphocyte
- chemokine
- autoimmune
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anti-mif
- glucocorticoid
- arthritis
- pulmonary
- artery
- leukocyte
- angiogenesis
- sepsis
-
rheumatoid
- tnf-alpha
- lipopolysaccharide
- factor-alpha
- myocardial
- t-cells
- atherosclerosis
-
chemotactic
-
c-reactive
- pituitary
-
chemoattractant
- infarct
-
lupus
- lymphokine
-
toll-like
-
autocrine
- cxcr2
-
synovial
- ifn-gamma
- il-1beta
-
counter-regulator
-
chemokine-like
- erythematosus
-
immunoregulatory
-
cell-mediated
- glomerulonephritis
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dehalogenation
-
tautomerization
-
counterregulates
-
delayed-type
-
pro-tumorigenic
- drug development
Reaction
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
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Engineering
Engineering on EC 5.3.2.1 - phenylpyruvate tautomerase
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K32A
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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
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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
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
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
P1A
E52Q
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mutation in alpha-subunit, 1.6fold increase in ratio of kcat to Km value
P1A
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mutation in beta-subunit, 8fold decrease in ratio of kcat to Km value
R11A
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mutation in alpha-subunit, 15fold decrease in ratio of kcat to Km value
R8A
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mutation in alpha-subunit, 19fold decrease in ratio of kcat to Km value
E52Q
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mutation in alpha-subunit, 1.6fold increase in ratio of kcat to Km value
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P1A
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mutation in beta-subunit, 8fold decrease in ratio of kcat to Km value
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R11A
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mutation in alpha-subunit, 15fold decrease in ratio of kcat to Km value
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R8A
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mutation in alpha-subunit, 19fold decrease in ratio of kcat to Km value
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additional information
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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
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for phenylenolpyruvate, the P1A mutant shows a 41fold decrease in kcat and a 14fold decrease in Km, resulting in an about 3fold decrease in kcat/Km. For (4-hydroxyphenyl)enolpyruvate, the P1A mutant shows a 16fold decrease in kcat, whereas the Km is not significantly affected, resulting in a 16fold decrease in kcat/Km. The P1A mutant has no detectable dehalogenase activity toward cis-3-chloroacrylate and trans-3-chloroacrylate, and no detectable activity toward 2-oxo-3-pentynoate (at pH 7.3)
P1A
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for phenylenolpyruvate, the P1A mutant shows a 41fold decrease in kcat and a 14fold decrease in Km, resulting in an about 3fold decrease in kcat/Km. For (4-hydroxyphenyl)enolpyruvate, the P1A mutant shows a 16fold decrease in kcat, whereas the Km is not significantly affected, resulting in a 16fold decrease in kcat/Km. The P1A mutant has no detectable dehalogenase activity toward cis-3-chloroacrylate and trans-3-chloroacrylate, and no detectable activity toward 2-oxo-3-pentynoate (at pH 7.3)
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