5.1.2.2: mandelate racemase
This is an abbreviated version!
For detailed information about mandelate racemase, go to the full flat file.
Word Map on EC 5.1.2.2
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5.1.2.2
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s-mandelate
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kenyon
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alpha-proton
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muconate
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gerlt
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1,1-proton
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benzohydroxamate
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petsko
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kozarich
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mitra
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galactarate
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benzoylformate
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d-glucarate
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ransom
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synthesis
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analysis
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biotechnology
- 5.1.2.2
- s-mandelate
-
kenyon
-
alpha-proton
- muconate
-
gerlt
-
1,1-proton
- benzohydroxamate
-
petsko
-
kozarich
- mitra
- galactarate
- benzoylformate
- d-glucarate
-
ransom
- synthesis
- analysis
- biotechnology
Reaction
Synonyms
mandelate racemase, mandelic acid racemase, mdlA, MR, racemase, mandelate
ECTree
5.1.2.2 mandelate racemaseAdvanced search results
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results (General Information
General Information on EC 5.1.2.2 - mandelate racemase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
mandelate racemase is a member of the enolase superfamily. The ability of the enzyme to form and deprotonate a Schiff-base intermediate furnishes a mechanistic link to other alpha/beta-barrel enzymes utilizing Schiff-base chemistry and is in accord with the sequence- and structure-based hypothesis that members of the metal-dependent enolase superfamily and the Schiff-base-forming N-acetylneuraminate lyase superfamily and aldolases share a common ancestor
physiological function
additional information
physiological function
enzyme catalyzes the Mg2+-dependent 1,1-proton transfer that interconverts the enantiomers of mandelate
physiological function
mandelate racemase catalyzes the interconversion of the enantiomers of mandelate
additional information
development and evaluation of a virtual mutant screening method based on the binding energy in the transition state, the method is beneficial in enzyme rational redesign and helps to better understand the catalytic properties of the enzyme, and it is effective in predicting the trend of mutational effects on catalysis, molecular dynamic simulation, overview
additional information
significance of Ser139 in mandelate racemization, the active site residue S139 forms a hydrogen bond with one carboxyl oxygen of the substrate mandelate, residues S139 and E317 of mandelate racemase have a synergistic effect on transition state stabilization, overview
additional information
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significance of Ser139 in mandelate racemization, the active site residue S139 forms a hydrogen bond with one carboxyl oxygen of the substrate mandelate, residues S139 and E317 of mandelate racemase have a synergistic effect on transition state stabilization, overview
additional information
the enzyme's 20s loop likely undergoes a significant conformational change upon binding (R)-mandelate
additional information
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the enzyme's 20s loop likely undergoes a significant conformational change upon binding (R)-mandelate
additional information
enzyme molecular dynamics simulation and molecular docking
additional information
role for the Broensted acid-base catalysts of mandelate racemase in transition state stabilization. Enzyme-catalyzed abstraction of an alpha-proton from a carbon acid substrate with a high pKa. Residues Lys166 and His297 play dual roles in catalysis: they act as Broensted acid-base catalysts, and they stabilize both the enolate moiety and phenyl ring of the altered substrate in the transition state
additional information
the thermal stability of mandelate racemase is investigated through molecular dynamics simulations in the temperature range of 30-90°C
additional information
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enzyme molecular dynamics simulation and molecular docking
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