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Information on EC 5.3.2.1 - phenylpyruvate tautomerase
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EC Tree
5.3.2.1 phenylpyruvate tautomeraseIUBMB Comments
Also acts on other arylpyruvates.
Specify your search results
Word Map
- 5.3.2.1
- necrosis
- monocyte
- tnf
- endothelial
- lymphocyte
- chemokine
- autoimmune
-
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
-
dehalogenation
-
tautomerization
-
counterregulates
-
delayed-type
-
pro-tumorigenic
- drug development
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
macrophage migration inhibitory factor, cis-caad, mif tautomerase, trans-3-chloroacrylic acid dehalogenase, cis-3-chloroacrylic acid dehalogenase, phenylpyruvate tautomerase, phenylpyruvate keto-enol tautomerase, macrophage migration inhibitory factor tautomerase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CaaD
cis-3-chloroacrylic acid dehalogenase
cis-CaaD
Macrophage migration inhibitory factor
MIF
phenyl(enol)pyruvate tautomerase
Phenylpyruvate keto-enol tautomerase
-
-
-
-
Phenylpyruvic keto-enol isomerase
-
-
-
-
PPT
Tautomerase, phenylpyruvate
-
-
-
-
CaaD
-
CaaD (trans-3-chloroacrylic acid dehalogenase) exhibits a robust phenylpyruvate tautomerase activity
CaaD
-
CaaD (trans-3-chloroacrylic acid dehalogenase) exhibits a robust phenylpyruvate tautomerase activity
-
Macrophage migration inhibitory factor
-
-
-
-
MIF
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Keto-phenylpyruvate = enol-phenylpyruvate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
tautomerization
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
phenylpyruvate keto---enol-isomerase
Also acts on other arylpyruvates.
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CAS REGISTRY NUMBER
COMMENTARY
9023-54-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-(3-hydroxyphenyl)pyruvate
2-hydroxy-3-(3-hydroxyphenyl)prop-2-enoate
-
keto-form
enol-form
?
4-(hydroxyphenyl)pyruvate
4-(hydroxyphenyl)pyruvate
enol form
keto form
-
?
trans-3-chloroacrylate
malonate semialdehyde + HCl
-
the reaction is performed by CAAD
-
-
?
(4-hydroxyphenyl)enolpyruvate
(4-hydroxyphenyl)pyruvate
-
-
-
-
?
(4-hydroxyphenyl)enolpyruvate
(4-hydroxyphenyl)pyruvate
-
-
-
-
?
2-oxo-3-pentynoate
acetopyruvate + ?
-
at pH 6.5, CCH2 exhibits hydratase activity and converts 2-oxo-3-pentynoate to acetopyruvate
-
-
?
2-oxo-3-pentynoate
acetopyruvate + ?
-
at pH 6.5, CCH2 exhibits hydratase activity and converts 2-oxo-3-pentynoate to acetopyruvate
-
-
?
3-(4-hydroxyphenyl)pyruvate
2-hydroxy-3-(4-hydroxyphenyl)prop-2-enoate
-
keto-form
-
-
?
3-(4-hydroxyphenyl)pyruvate
2-hydroxy-3-(4-hydroxyphenyl)prop-2-enoate
-
keto-form
-
-
?
3-(4-hydroxyphenyl)pyruvate
2-hydroxy-3-(4-hydroxyphenyl)prop-2-enoate
-
keto-form
-
-
?
3-(4-hydroxyphenyl)pyruvate
2-hydroxy-3-(4-hydroxyphenyl)prop-2-enoate
-
keto-form
-
-
?
3-(4-hydroxyphenyl)pyruvate
2-hydroxy-3-(4-hydroxyphenyl)prop-2-enoate
-
keto-form
-
-
?
3-(4-hydroxyphenyl)pyruvate
2-hydroxy-3-(4-hydroxyphenyl)prop-2-enoate
-
keto-form
-
-
?
3-(4-hydroxyphenyl)pyruvate
2-hydroxy-3-(4-hydroxyphenyl)prop-2-enoate
-
keto-form
-
-
?
3-(4-hydroxyphenyl)pyruvate
2-hydroxy-3-(4-hydroxyphenyl)prop-2-enoate
-
keto-form
-
-
?
3-(4-hydroxyphenyl)pyruvate
2-hydroxy-3-(4-hydroxyphenyl)prop-2-enoate
-
keto-form
-
-
?
3-(4-hydroxyphenyl)pyruvate
2-hydroxy-3-(4-hydroxyphenyl)prop-2-enoate
-
keto-form
-
-
?
3-(4-hydroxyphenyl)pyruvate
2-hydroxy-3-(4-hydroxyphenyl)prop-2-enoate
-
keto-form
enol-form
?
cis-3-chloroacrylate
malonate semialdehyde + HCl
-
the reaction is performed by cis-CAAD
-
-
?
cis-3-chloroacrylate
malonate semialdehyde + HCl
-
the reaction is performed by cis-CAAD
-
-
?
enol-(p-hydroxyphenyl)pyruvate
keto-(p-hydroxyphenyl)pyruvate
-
-
r
enol-phenylpyruvate
keto-phenylpyruvate
-
-
reaction is stereoselective, generating the (3R) isomer of [3-D]phenylpyruvate in D2O in a ratio of 6.6:1
-
?
enol-phenylpyruvate
keto-phenylpyruvate
-
reaction is stereoselective, generating the 3S isomer of [3-D]phenylpyruvate in a 18:1 ratio in D2O
-
-
?
enol-phenylpyruvate
keto-phenylpyruvate
-
reaction is stereoselective, generating the 3S isomer of [3-D]phenylpyruvate in a 18:1 ratio in D2O
-
-
?
keto-(p-hydroxyphenyl)pyruvate
enol-(p-hydroxyphenyl)pyruvate
the substrate interacts with Pro1, Lys32 and Ile64 from one subunit and Tyr95 and Asn97 from an adjacent subunit
-
?
keto-(p-hydroxyphenyl)pyruvate
enol-(p-hydroxyphenyl)pyruvate
-
-
r
Phenylpyruvate
Phenylpyruvate
-
converts the enol-form to the keto-form by incorporating a solvent proton into the pro-R position, in the reverse reaction the same pro-R proton is abstracted
enol-form
?
additional information
?
-
the enzyme is chemotactic for human monocytes and activates them to produce IL-8, TNF-alpha and endogenous MIF
-
?
additional information
?
-
-
the enzyme is chemotactic for human monocytes and activates them to produce IL-8, TNF-alpha and endogenous MIF
-
?
additional information
?
-
important immunoregulatory molecule with a unique ability to suppress the anti-inflammatory effects of glucocorticoids
-
?
additional information
?
-
-
MIF is a homotrimeric multifunctional proinflammatory cytokine. It also shows dopachrome tautomerase activity. Binding of MIF to its receptor, CD74, overview
-
-
?
additional information
?
-
-
the MIF protein is multifunctional, exhibiting besides its tautomerase activity, e.g. also L-dopachrome isomerase activity, EC 5.3.3.12, and thioredoxin-like function, or its cytokine function, overview
-
-
?
additional information
?
-
-
the N-terminal Pro is essential for the tautomerase activity of MIF
-
-
?
additional information
?
-
-
the enzymatic activity of macrophage migration inhibitory factor does not play a role in its migration inhibiting properties. Macrophage migration inhibitory factor is an inhibitor of the random migration of monocytes and macrophages and has since been proposed to have a number of immune and catalytic functions, macrophage migration inhibitory factor is an inhibitor of monocyte chemoattractant protein 1-induced chemotaxis of human peripheral blood monocytes
-
?
additional information
?
-
-
CCH2 functions as an efficient PPT and exhibits low-level promiscuous dehalogenase activity, processing both cis- and trans-3-chloroacrylic acid
-
-
?
additional information
?
-
-
CCH2 functions as an efficient PPT and exhibits low-level promiscuous dehalogenase activity, processing both cis- and trans-3-chloroacrylic acid
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
the enzyme is chemotactic for human monocytes and activates them to produce IL-8, TNF-alpha and endogenous MIF
-
?
additional information
?
-
-
the enzyme is chemotactic for human monocytes and activates them to produce IL-8, TNF-alpha and endogenous MIF
-
?
additional information
?
-
important immunoregulatory molecule with a unique ability to suppress the anti-inflammatory effects of glucocorticoids
-
?
additional information
?
-
-
MIF is a homotrimeric multifunctional proinflammatory cytokine. It also shows dopachrome tautomerase activity. Binding of MIF to its receptor, CD74, overview
-
-
?
additional information
?
-
-
the MIF protein is multifunctional, exhibiting besides its tautomerase activity, e.g. also L-dopachrome isomerase activity, EC 5.3.3.12, and thioredoxin-like function, or its cytokine function, overview
-
-
?
additional information
?
-
-
the enzymatic activity of macrophage migration inhibitory factor does not play a role in its migration inhibiting properties. Macrophage migration inhibitory factor is an inhibitor of the random migration of monocytes and macrophages and has since been proposed to have a number of immune and catalytic functions, macrophage migration inhibitory factor is an inhibitor of monocyte chemoattractant protein 1-induced chemotaxis of human peripheral blood monocytes
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1E,6E)-1-(4-hydroxy-3-methoxyphenyl)-7-(4-hydroxyphenyl)hepta-1,6-diene-3,5-dione
-
-
2,2-dimethylpropyl [3-(3-fluoro-4-hydroxyphenyl)-4,5-dihydro-1,2-oxazol-5-yl]acetate
-
-
2,4,6-trimethylphenyl [3-(4-hydroxyphenyl)-4,5-dihydro-1,2-oxazol-5-yl]acetate
-
-
2-Oxo-3-pentynoate
-
at pH 8.5, CCH2 is inactivated by 2-oxo-3-pentynoate due to the covalent modification of Pro-1
2-oxo-4-phenyl-3-butynoate
irreversible inactivation by covalent modifiaction of N-terminal proline residue via a Michael-addition of proline to C4 of the inhibitor
2-[3,6-bis(diethylamino)-3H-xanthen-9-yl]-5-[(6-{[4-({[3-(4-hydroxyphenyl)-4,5-dihydro-1,2-oxazol-5-yl]acetyl}amino)butyl]amino}-6-oxohexyl)sulfamoyl]benzenesulfonic acid
-
-
2-[3-(4-hydroxyphenyl)-4,5-dihydro-1,2-oxazol-5-yl]-N-(4-methoxyphenyl)acetamide
-
-
AV1013
-
noncompetitive inhibitor of the p-hydroxyphenylpyruvate tautomerase activity of MIF
AV411
-
ibudilast, i.e. 3-isobutyryl-2-isopropylpyrazolo-[1,5-a]pyridine, noncompetitive inhibitor of the p-hydroxyphenylpyruvate tautomerase activity of MIF
AVP-13546
-
inhibits the tautomerase activity of MIF and reduces cytokine, including TNF-alpha, levels in vivo
-
Benzyl isothiocyanate
-
specific inhibition of MIF tautomerase activity is mediated by selective modification of the N-terminal proline
caffeic acid
-
IC50 ketonase reaction 0.5 microM, pH 6.5, room temperatur, IC50 enolase reaction 2.0 microM, pH 6.2, room temperatur
Cinnamic acid
-
IC50 ketonase reaction 20.9 microM, pH 6.5, room temperatur, IC50 enolase reaction 229.6 microM, pH 6.2, room temperatur
ethyl 7-hydroxy-2-oxo-2H-chromene-3-carboxylate
-
inhibition mechanism, overview
folic acid
-
IC50 ketonase reaction 62.7 microM, pH 6.5, room temperatur, IC50 enolase reaction 80.2 microM, pH 6.2, room temperatur
galangin
-
IC50 ketonase reaction 36.9 microM, pH 6.5, room temperatur, IC50 enolase reaction 143.7 microM, pH 6.2, room temperatur
Ibuprofen
-
IC50 ketonase reaction 10334.3, pH 6.5, room temperatur, IC50 enolase reaction 109.6 microM, pH 6.2, room temperatur
isoeugenol
-
IC50 ketonase reaction 50.4 microM, pH 6.5, room temperatur, IC50 enolase reaction 129.0 microM, pH 6.2, room temperatur
methotrexate
-
IC50 ketonase reaction 15.6 microM, pH 6.5, room temperatur, IC50 enolase reaction 63.7 microM, pH 6.2, room temperatur
N-(4-aminobutyl)-2-[3-(4-hydroxyphenyl)-4,5-dihydro-1,2-oxazol-5-yl]acetamide
-
-
o-coumaric acid
-
IC50 ketonase reaction 87.8 microM, pH 6.5, room temperatur, IC50 enolase reaction 175.7 microM, pH 6.2, room temperatur
p-coumaric acid
-
IC50 ketonase reaction 18.1 microM, pH 6.5, room temperatur, IC50 enolase reaction 103.3 microM, pH 6.2, room temperatur
Phenylbutazone
-
IC50 ketonase reaction 7126.7 microM, pH 6.5, room temperatur, IC50 enolase reaction 376.6 microM, pH 6.2, room temperatur
piroxicam
-
IC50 ketonase reaction 120.9 microM, pH 6.5, room temperatur, IC50 enolase reaction 74.8 microM, pH 6.2, room temperatur
Quinine
-
IC50 ketonase reaction 34.9 microM, pH 6.5, room temperatur, IC50 enolase reaction 156.3 microM, pH 6.2, room temperatur
tert-butyl [4-({[3-(4-hydroxyphenyl)-4,5-dihydro-1,2-oxazol-5-yl]acetyl}amino)butyl]carbamate
-
-
(S,R)-3-(4-hydroxyphenyl)-4,5-dihydro-5-isoxazole acetic acid methyl ester
-
i.e. ISO-I
acetaminophen
-
IC50 ketonase reaction 1.0 microM, pH 6.5, room temperatur, IC50 enolase reaction 2.6 microM, pH 6.2, room temperatur
boldine
-
IC50 ketonase reaction 5.7 microM, pH 6.5, room temperatur, IC50 enolase reaction 77.9 microM, pH 6.2, room temperatur
carnosic acid
-
IC50 ketonase reaction 15.5 microM, pH 6.5, room temperatur, IC50 enolase reaction 115.8 microM, pH 6.2, room temperatur
chlorogenic acid
-
IC50 ketonase reaction 7.6 microM, pH 6.5, room temperatur, IC50 enolase reaction 127.0 microM, pH 6.2, room temperatur
curcumin
-
IC50 ketonase reaction 0.7 microM, pH 6.5, room temperatur, IC50 enolase reaction 12.2 microM, pH 6.2, room temperatur
ferulic acid
-
IC50 ketonase reaction 31.7 microM, pH 6.5, room temperatur, IC50 enolase reaction 85.3 microM, pH 6.2, room temperatur
phloretin
-
IC50 ketonase reaction 4.8 microM, pH 6.5, room temperatur, IC50 enolase reaction 84.1 microM, pH 6.2, room temperatur
resveratrol
-
IC50 ketonase reaction 1.9 microM, pH 6.5, room temperatur, IC50 enolase reaction 28.0 microM, pH 6.2, room temperatur
rosmarinic acid
-
IC50 ketonase reaction 13.8 microM, pH 6.5, room temperatur, IC50 enolase reaction 65.6 microM, pH 6.2, room temperatur
umbelliferone
-
IC50 ketonase reaction 2.6 microM, pH 6.5, room temperatur, IC50 enolase reaction 19.5 microM, pH 6.2, room temperatur
additional information
-
50% inhibition could not be attained: estragol, gentisic acid, tropolone
-
additional information
-
design and synthesis of irreversible isothiocyanate-based inhibitors of MIF, inhibitory potencies and inhibition mechanism, overview
-
additional information
-
there exist several classes of inhibitors that are active against MIF tautomerase activity, overview. No activity by (S,R)-3-(4-methoxyphenyl)-4,5-dihydro-5-isoxazole acetic acid methyl ester and isoxazole and its reduced derivative
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.152
cis-3-chloroacrylate
-
wild type enzyme cis-CAAD, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
96
trans-3-chloroacrylate
-
wild type enzyme CCH2, in in 50 mM Tris-SO4 buffer (pH 8.0), at 22°C
0.79
(4-hydroxyphenyl)enolpyruvate
-
wild type enzyme CCH2-P1A, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
0.89
(4-hydroxyphenyl)enolpyruvate
-
wild type enzyme CCH2, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
0.11
phenylenolpyruvate
-
wild type enzyme cis-CAAD, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
0.25
phenylenolpyruvate
-
mutant enzyme CCH2-P1A, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
3.5
phenylenolpyruvate
-
wild type enzyme CCH2, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.6
cis-3-chloroacrylate
-
wild type enzyme cis-CAAD, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
0.0004
trans-3-chloroacrylate
-
wild type enzyme CCH2, in in 50 mM Tris-SO4 buffer (pH 8.0), at 22°C
0.2
(4-hydroxyphenyl)enolpyruvate
-
wild type enzyme CCH2-P1A, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
3.2
(4-hydroxyphenyl)enolpyruvate
-
wild type enzyme CCH2, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
0.2
phenylenolpyruvate
-
wild type enzyme cis-CAAD, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
0.8
phenylenolpyruvate
-
mutant enzyme CCH2-P1A, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
34
phenylenolpyruvate
-
wild type enzyme CCH2, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4
trans-3-chloroacrylate
-
wild type enzyme CCH2, in in 50 mM Tris-SO4 buffer (pH 8.0), at 22°C
2.5
(4-hydroxyphenyl)enolpyruvate
-
wild type enzyme CCH2-P1A, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
3.5
(4-hydroxyphenyl)enolpyruvate
-
wild type enzyme CCH2, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
1.6
cis-3-chloroacrylate
-
wild type enzyme CCH2, in in 50 mM Tris-SO4 buffer (pH 8.0), at 22°C
30
cis-3-chloroacrylate
-
wild type enzyme cis-CAAD, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
1.8
phenylenolpyruvate
-
wild type enzyme cis-CAAD, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
3.3
phenylenolpyruvate
-
mutant enzyme CCH2-P1A, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
9.8
phenylenolpyruvate
-
wild type enzyme CCH2, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0241
(S,R)-3-(4-hydroxyphenyl)-4,5-dihydro-5-isoxazole acetic acid methyl ester
-
pH and temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0062
(3Z)-3-[4-(dimethylamino)benzylidene]-7-hydroxy-2H-chromene-2,4(3H)-dione
Homo sapiens
-
-
0.007
(R)-3-(4-hydroxyphenyl)-4,5-dihydro-5-isoxazole acetic acid methyl ester
Homo sapiens
-
-
0.013
(S)-3-(4-hydroxyphenyl)-4,5-dihydro-5-isoxazole acetic acid methyl ester
Homo sapiens
-
-
0.0015
3-[4-(1,3-benzodioxol-5-yl)-1,3-thiazol-2-yl]-7-hydroxy-2H-chromen-2-one
Homo sapiens
-
-
0.00028
7-hydroxy-3-[4-(2-oxo-2H-chromen-3-yl)-1,3-thiazol-2-yl]-2H-chromen-2-one
Homo sapiens
-
-
0.0005 - 0.002
caffeic acid
Bos taurus
-
IC50 ketonase reaction 0.5 microM, pH 6.5, room temperatur, IC50 enolase reaction 2.0 microM, pH 6.2, room temperatur
0.0209 - 0.2296
Cinnamic acid
Bos taurus
-
IC50 ketonase reaction 20.9 microM, pH 6.5, room temperatur, IC50 enolase reaction 229.6 microM, pH 6.2, room temperatur
0.0181 - 0.1033
p-coumaric acid
Bos taurus
-
IC50 ketonase reaction 18.1 microM, pH 6.5, room temperatur, IC50 enolase reaction 103.3 microM, pH 6.2, room temperatur
3.6241
parthenolide
Bos taurus
-
IC50 ketonase reaction 3624.1 microM, pH 6.5, room temperatur
0.0026 - 0.0195
umbelliferone
Bos taurus
-
IC50 ketonase reaction 2.6 microM, pH 6.5, room temperatur, IC50 enolase reaction 19.5 microM, pH 6.2, room temperatur
0.0155
carnosic acid
Bos taurus
-
IC50 ketonase reaction 15.5 microM, pH 6.5, room temperatur
0.1158
carnosic acid
Bos taurus
-
IC50 enolase reaction 115.8 microM, pH 6.2, room temperatur
0.0076
chlorogenic acid
Bos taurus
-
IC50 ketonase reaction 7.6 microM, pH 6.5, room temperatur
0.127
chlorogenic acid
Bos taurus
-
IC50 enolase reaction 127.0 microM, pH 6.2, room temperatur
10.3343
Ibuprofen
Bos taurus
-
IC50 ketonase reaction 10334.3 microM, pH 6.5, room temperatur
0.0878
o-coumaric acid
Bos taurus
-
IC50 ketonase reaction 87.8 microM, pH 6.5, room temperatur
0.1757
o-coumaric acid
Bos taurus
-
IC50 enolase reaction 175.7 microM, pH 6.2, room temperatur
0.3766
Phenylbutazone
Bos taurus
-
IC50 enolase reaction 376.6 microM, pH 6.2, room temperatur
7.1267
Phenylbutazone
Bos taurus
-
IC50 ketonase reaction 7126.7 microM, pH 6.5, room temperatur
0.0138
rosmarinic acid
Bos taurus
-
IC50 ketonase reaction 13.8 microM, pH 6.5, room temperatur
0.0656
rosmarinic acid
Bos taurus
-
IC50 enolase reaction 65.6 microM, pH 6.2, room temperatur
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
trans-3-chloroacrylic acid dehydrogenase CaaD has phenylpyruvate tautomerase activity
-
-
brenda
trans-3-chloroacrylic acid dehydrogenase CaaD has phenylpyruvate tautomerase activity
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
MIF expression contributes to cell proliferation, invasiveness and neo-angiogenesis of neuroblastoma, gastric, hepatocellularbladder, and breast carcinomas. MIF takes part in the pathogenesis of Alzheimer's disease and multiple sklerosis
malfunction
-
MIF is implicated in the pathogenesis of several inflammatory and autoimmune diseases
physiological function
-
MIF is involved in diverse biological processes, e.g. MIF glucocorticoid overriding activity, endotoxin lipopolysaccharide-induced TNF production, MIF-mediated stimulation of ERK1/2 MAP kinase and proliferation of serum-starved cells, MIF-mediated upregulation of arachidonic acid in macrophages, and Cox-2 activation
physiological function
-
MIF plays an essential role in both, innate and adaptive immune response. It is implicated in tumor growth and angiogenesis, an exerts an antagonistic effect against glucocorticoid immunosuppressive action, and shows glucorticoid overriding activity
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MIFH_BRUMA
115
0
12320
Swiss-Prot
other Location (Reliability: 2)
MIFH_TRISP
114
0
12337
Swiss-Prot
other Location (Reliability: 2)
MIFH_TRITR
114
0
12043
Swiss-Prot
other Location (Reliability: 1)
MIFH_WUCBA
115
0
12364
Swiss-Prot
other Location (Reliability: 1)
MIF_BOVIN
115
0
12343
Swiss-Prot
other Location (Reliability: 2)
MIF_CHICK
115
0
12484
Swiss-Prot
other Location (Reliability: 1)
MIF_HUMAN
115
0
12476
Swiss-Prot
other Location (Reliability: 2)
MIF_MACFA
115
0
12476
Swiss-Prot
other Location (Reliability: 2)
MIF_MACMU
115
0
12476
Swiss-Prot
other Location (Reliability: 2)
MIF_MERUN
115
0
12449
Swiss-Prot
other Location (Reliability: 2)
MIF_MOUSE
115
0
12504
Swiss-Prot
other Location (Reliability: 2)
MIF_PIG
115
0
12451
Swiss-Prot
other Location (Reliability: 3)
MIF_RAT
115
0
12477
Swiss-Prot
other Location (Reliability: 2)
MIF_SHEEP
115
0
12343
Swiss-Prot
other Location (Reliability: 2)
MIF_XENLA
115
0
12500
Swiss-Prot
other Location (Reliability: 2)
MIF_XENTR
115
0
12524
Swiss-Prot
other Location (Reliability: 2)
A0A8B6E3V3_MYTGA
115
0
12709
TrEMBL
other Location (Reliability: 2)
A0A451FY67_MYTGA
111
0
12641
TrEMBL
other Location (Reliability: 4)
W2E2Y0_9BACL
445
0
48209
TrEMBL
-
A0A173WWE7_9BIFI
115
0
12657
TrEMBL
-
A0A2I0BHK3_9ASPA
121
0
13010
TrEMBL
other Location (Reliability: 2)
A0A060S140_PLARE
116
0
12811
TrEMBL
other Location (Reliability: 1)
A0A7C8YNF7_OPUST
115
0
12128
TrEMBL
other Location (Reliability: 3)
A0A0B2PML7_GLYSO
107
0
11174
TrEMBL
other Location (Reliability: 3)
A0A0H3E833_BIFBP
Bifidobacterium bifidum (strain PRL2010)
115
0
12586
TrEMBL
-
A0A0B2SJ75_GLYSO
112
0
12339
TrEMBL
other Location (Reliability: 3)
A0A7C9E7H7_OPUST
113
0
12060
TrEMBL
other Location (Reliability: 2)
Q0ZBR7_DANRE
115
0
12412
TrEMBL
other Location (Reliability: 2)
G4SZ39_META2
Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z)
115
0
12607
TrEMBL
-
A0A023B961_GRENI
115
0
11944
TrEMBL
other Location (Reliability: 1)
I2CSA6_NANGC
Nannochloropsis gaditana (strain CCMP526)
171
0
18096
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0B2RIX7_GLYSO
112
0
12314
TrEMBL
other Location (Reliability: 3)
A0A0B2QG49_GLYSO
115
0
12002
TrEMBL
other Location (Reliability: 2)
A0A2G9HZQ9_9LAMI
90
0
9656
TrEMBL
other Location (Reliability: 2)
A0A7C8YND5_OPUST
103
0
10827
TrEMBL
other Location (Reliability: 3)
A0A2L1UCG1_9BACL
445
0
48209
TrEMBL
-
B2J6C9_NOSP7
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
117
0
12874
TrEMBL
-
Q8I5C5_PLAF7
116
0
12845
TrEMBL
other Location (Reliability: 1)
A0A0B2QRA3_GLYSO
115
0
12358
TrEMBL
other Location (Reliability: 3)
M2XLC2_GALSU
114
0
12423
TrEMBL
other Location (Reliability: 2)
V9W2K4_9BACL
421
0
45357
TrEMBL
-
A0A1Z5JYI9_FISSO
132
0
13953
TrEMBL
other Location (Reliability: 2)
A0A2G9HZR1_9LAMI
115
0
12138
TrEMBL
other Location (Reliability: 3)
K5AAY4_PAEA2
Paenibacillus alvei (strain ATCC 6344 / DSM 29 / NBRC 3343 / NCIMB 9371 / NCTC 6352)
381
0
40769
TrEMBL
-
K8YZJ3_NANGC
Nannochloropsis gaditana (strain CCMP526)
184
1
19685
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7C9CHL3_OPUST
103
0
10886
TrEMBL
other Location (Reliability: 2)
Q0ZBS0_SALSA
114
0
12369
TrEMBL
other Location (Reliability: 2)
A0A1J1HBD4_PLARL
116
0
12969
TrEMBL
other Location (Reliability: 1)
W6M9Z9_9GAMM
115
0
12292
TrEMBL
-
A0A2G9GUA2_9LAMI
115
0
12181
TrEMBL
other Location (Reliability: 3)
A0A2G9G8Z7_9LAMI
115
0
12134
TrEMBL
other Location (Reliability: 4)
A0A6J8BRS2_MYTCO
425
0
47203
TrEMBL
other Location (Reliability: 2)
A9BB73_PROM4
Prochlorococcus marinus (strain MIT 9211)
112
0
12441
TrEMBL
-
A0A2G9GUA4_9LAMI
115
0
12263
TrEMBL
other Location (Reliability: 3)
B9SL16_RICCO
115
0
12045
TrEMBL
other Location (Reliability: 2)
A0A2G9G8Y2_9LAMI
112
0
12083
TrEMBL
other Location (Reliability: 2)
A0A1Z5JNU3_FISSO
165
0
17630
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0B2SKT7_GLYSO
115
0
12047
TrEMBL
other Location (Reliability: 3)
A0A0B2PYA1_GLYSO
248
0
27214
TrEMBL
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12000
12316
-
x * 12316, mutant enzyme K32A, electrospray ionization mass spectrometry
12335
x * 12335, electrospray ionization mass spectrometry, mutant enzyme P1G
12347
12358
x * 12358, electrospray ionization mass spectrometry, mutant enzyme Y95F
12371
12401
-
x * 12401, mutant enzyme K32R, electrospray ionization mass spectrometry
12347
x * 12347, electrospray ionization mass spectrometry, mutant enzyme N97A
12347
x * 12347, electrospray ionization mass spectrometry, mutant enzyme P1A
12371
x * 12371, electrospray ionization mass spectrometry, wild-type enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterohexamer
homotrimer
trimer
?
x * 12335, electrospray ionization mass spectrometry, mutant enzyme P1G
?
x * 12347, electrospray ionization mass spectrometry, mutant enzyme N97A
?
x * 12347, electrospray ionization mass spectrometry, mutant enzyme P1A
?
x * 12358, electrospray ionization mass spectrometry, mutant enzyme Y95F
homotrimer
-
3 * 16093, electrospray ionization mass spectrometry
homotrimer
-
3 * 16093, electrospray ionization mass spectrometry
-
trimer
-
the tertiary structure is stabilized by hydrogen bonds and a hydrophobic core, three beta-sheets and six alpha-helices surround a traversing channel with dominant positive charge in the middle of the trimer, structure, overview. The enzyme contains a Cys-Xaa-Xaa-Cys motif required for oxido-reductase activity and MIF-like activities like glucorticoid overriding and cell proliferation
trimer
-
trimer formation is required for MIF tautomerase activity, trimer three-dimensional structure and tautomerase active site structure. The subunit interface is not as hydrophobic as the interior of the monomer, however, there is a hydrophobic patch on the surface involving residues Y36, Y95, W108, and F113, MALDI-TOF and analytical gel filtration analysis, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure of Bm-MIF-2 at 1.8 A resolution reveals a trimeric assembly with an inner pore created by beta-stranded sheets from each subunit
hanging drop vapor diffusion method, crystal structure of the enzyme complexed with p-hydroxyphenylpyruvate
MIF is cocrystallized with the R-isomer of AV1013 alone and with the substrate enol-(p-hydroxyphenyl)pyruvate
-
crystal structure of a complex between enzyme and the competitive inhibitor (E)-2-fluoro-o-hydroxycinnamate determined to 1.8 A resolution
crystallization of the Y95F mutant enzyme by hanging drop vapor diffusion method, crystal structure of the enzyme with the competitive inhibitor (E)-2-fluoro-p-hydroxycinnamate bound at the active site and that of the protein complexed with the enol form of (p-hydroxyphenyl)pyruvate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
-
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
P1A
-
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
-
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, protein from homogenated tissue heated to 58°C for 20 min, and subsequently salted out of the supernatant with ammonium sulfate to the final saturation of 80% can be stored six months without loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant MIF from Escherichia coli strain BL21(DE3) by anion exchange chromatography and gel filtration
-
simple method for purification based on size-exclusion chromatography on Toyopearl TSK polymer having a tendencey to adsorb the enzyme
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzymes P1G, P1A, Y95F and N97A, expression in Escherichia coli BL21
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
MIF expression is upregulated by cytokines, TNF-alpha and interleukin-I, and by bacterial endotoxins, such as lipopolysaccharides, and exotoxins
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
the tautomerase activity of MIF is a target for inhibitor development, overview
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Knox, W.E.; Pitt, B.M.
Enzymic catalysis of the keto-enol tautomerization of phenylpyruvic acids
J. Biol. Chem.
225
675-688
1957
Bos taurus, Canis lupus familiaris, Cavia porcellus, Equus caballus, Neurospora sp., no activity in Aerobacter sp., Oryctolagus cuniculus, Pseudomonas sp., Rattus norvegicus, Sus scrofa
brenda
Blasi, F.; Fragomele, F.; Covelli, I.
Thyroidal phenylpyruvate tautomerase
J. Biol. Chem.
244
4864-4870
1969
Sus scrofa
brenda
Knox, W.E.
p-Hydroxyphenylpyruvate enol-keto tautomerase
Methods Enzymol.
2
289-292
1955
Sus scrofa
-
brenda
Retey, J.; Bartl, K.; Ripp, E.; Hull, W.E.
Stereospecificity of phenylpyruvate tautomerase. A convenient method for the preparation of chirally labelled phenylpyruvates
Eur. J. Biochem.
72
251-257
1977
Bos taurus
brenda
Pirrung, M.C.; Chen, J.; Rowley, E.G.; McPhall, A.T.
Mechanistic and stereochemical study of phenylpyruvate tautomerase
J. Am. Chem. Soc.
115
7103-7110
1993
Sus scrofa
-
brenda
Rosengarten, E.; Aman, P.; Thelin, S.; Hansson, C.; Ahlfors, S.; Bjoerk, P.; Jacobson, L.; Rorsman, H.
The macrophage inhibitory factor MIF is a phenylpyruvate tautomerase
FEBS Lett.
417
85-88
1997
Bos taurus, Homo sapiens
brenda
Hermanowski-Vosatka, A.; Mundt, S.S.; Ayala, J.M.; Goyal, S.; Hanlon, W.A.; Czerwinski, R.M.; Wright, S.D.; Whitman, C.P.
Enzymatically inactive macrophage migration inhibitory factor inhibits monocyte chemotaxis and random migration
Biochemistry
38
12841-12849
1999
Mus musculus
brenda
Johnson, W.H., Jr.; Czerwinski, R.M.; Stamps, S.L.; Whitman, C.P.
A kinetic and stereochemical investigation of the role of lysine-32 in the phenylpyruvate tautomerase activity catalyzed by macrophage migration inhibitory factor
Biochemistry
38
16024-16033
1999
Mus musculus
brenda
Lubetsky, J.B.; Swope, M.; Dealwis, C.; Blake, P.; Lolis, E.
Pro-1 of macrophage migration inhibitory factor functions as a catalytic base in the phenylpyruvate tautomerase activity
Biochemistry
38
7346-7354
1999
Homo sapiens (P14174)
brenda
Taylor, A.B.; Johnson, W.H., Jr.; Czerwinski, R.M.; Li, H.S.; Hackert, M.L.; Whitman, C.P.
Crystal structure of macrophage migration inhibitory factor complexed with (E)-2-fluoro-p-hydroxycinnamate at 1.8 A resolution: implications for enzymatic catalysis and inhibition
Biochemistry
38
7444-7452
1999
Mus musculus (P34884), Mus musculus
brenda
Stamps, S.L.; Taylor, A.B.; Wang, S.C.; Hackert, M.L.; Whitman, C.P.
Mechanism of the phenylpyruvate tautomerase activity of macrophage migration inhibitory factor: properties of the P1G, P1A, Y95F, and N97A mutants
Biochemistry
39
9671-9678
2000
Mus musculus (P34884)
brenda
Zang, X.; Taylor, P.; Wang, J.M.; Meyer, D.J.; Scott, A.L.; Walkinshaw, M.D.; Maizels, R.M.
Homologues of human macrophage migration inhibitory factor from a parasitic nematode. Gene cloning, protein activity, and crystal structure
J. Biol. Chem.
277
44261-44267
2002
Brugia malayi (Q9NAS2), Brugia malayi
brenda
Molnar, V.; Garai, J.
Plant-derived anti-inflammatory compounds affect MIF tautomerase activity
Int. Immunopharmacol.
5
849-856
2005
Bos taurus
brenda
Poelarends, G.J.; Johnson, W.H.; Serrano, H.; Whitman, C.P.
Phenylpyruvate tautomerase activity of trans-3-chloroacrylic acid dehalogenase: evidence for an enol intermediate in the dehalogenase reaction?
Biochemistry
46
9596-9604
2007
Mus musculus, Pseudomonas pavonaceae, Pseudomonas pavonaceae 170
brenda
Cherepkova, O.A.; Lyutova, E.M.; Gurvits, B.Y.
Macrophage migration inhibitory factor: isolation from bovine brain
Biochemistry (Moscow)
71
73-78
2006
Bos taurus
brenda
Golubkov, P.A.; Johnson, W.H.; Czerwinski, R.M.; Person, M.D.; Wang, S.C.; Whitman, C.P.; Hackert, M.L.
Inactivation of the phenylpyruvate tautomerase activity of macrophage migration inhibitory factor by 2-oxo-4-phenyl-3-butynoate
Bioorg. Chem.
34
183-199
2006
Mus musculus (P34884)
brenda
Garai, J.; Molnar, V.; Eros, D.; Orfi, L.; Lorand, T.
MIF tautomerase inhibitor potency of alpha,beta-unsaturated cyclic ketones
Int. Immunopharmacol.
7
1741-1746
2007
Bos taurus
brenda
Poelarends, G.J.; Veetil, V.P.; Whitman, C.P.
The chemical versatility of the beta-alpha-beta fold: catalytic promiscuity and divergent evolution in the tautomerase superfamily
Cell. Mol. Life Sci.
65
3606-3618
2008
Pseudomonas pavonaceae, Pseudomonas pavonaceae 170
brenda
Ouertatani-Sakouhi, H.; El-Turk, F.; Fauvet, B.; Roger, T.; Le Roy, D.; Karpinar, D.P.; Leng, L.; Bucala, R.; Zweckstetter, M.; Calandra, T.; Lashuel, H.A.
A new class of isothiocyanate-based irreversible inhibitors of macrophage migration inhibitory factor
Biochemistry
48
9858-9870
2009
Homo sapiens
brenda
Garai, J.; Lorand, T.
Macrophage migration inhibitory factor (MIF) tautomerase inhibitors as potential novel anti-inflammatory agents: current developments
Curr. Med. Chem.
16
1091-1114
2009
Homo sapiens
brenda
Baas, B.J.; Zandvoort, E.; Wasiel, A.A.; Quax, W.J.; Poelarends, G.J.
Characterization of a newly identified mycobacterial tautomerase with promiscuous dehalogenase and hydratase activities reveals a functional link to a recently diverged cis-3-chloroacrylic acid dehalogenase
Biochemistry
50
2889-2899
2011
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc(2)155
brenda
Cho, Y.; Crichlow, G.V.; Vermeire, J.J.; Leng, L.; Du, X.; Hodsdon, M.E.; Bucala, R.; Cappello, M.; Gross, M.; Gaeta, F.; Johnson, K.; Lolis, E.J.
Allosteric inhibition of macrophage migration inhibitory factor revealed by ibudilast
Proc. Natl. Acad. Sci. USA
107
11313-11318
2010
Homo sapiens
brenda
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