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 (Inhibitors
Inhibitors on EC 5.1.2.2 - mandelate racemase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(R,S)-1-hydroxyethylphosphonate
transition state analogue inhibitor
(R,S)-2,2,2-trifluoro-1-hydroxyethylphosphonate
transition state analogue inhibitor
3,3,3-trifluoro-2-hydroxy-2-(trifluoromethyl)-propanoate
a substrate-product analogue and a potent competitive inhibitor with both (R)-mandelate and (R)-trifluorolactate. The inhibitor exhibits a different binding mode with the two trifluoromethyl groups closely packed against the 20s loop and the carboxylate bridging the two active site Broensted acid-base catalysts Lys166 and His297
3-hydroxypyruvate
an irreversible, time-dependent inhibitor, causes inactivation of mandelate racemase. Protection from inactivation by the competitive inhibitor benzohydroxamate. 3-Hydroxypyruvate undergoes Schiff-base formation with Lys166 at the active site, followed by formation of an aldehyde/enol(ate) adduct
N-hydroxyformanilide
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potent competitive inhibitor, MR can bind either the protonated or deprotonated forms of N-hydroxyformanilide, with a 10fold greater affinity for the latter form
(R,S)-alpha-hydroxybenzylphosphonate
transition state analogue inhibitor
benzohydroxamate
a reasonable mimic of the transition state and/or intermediate that chelates the active site divalent metal ion and is bound in a conformation with the phenyl ring coplanar with the hydroxamate moiety, active site binding, structure comparison with bound Cupferron, overview
benzohydroxamate
BzH, the enzyme binds the intermediate/transition state analogue inhibitor in an entropy-driven process, consistent with an increased number of hydrophobic interactions, additional specific interactions contribute to binding, detailed kinetics and binding analysis, overview
Cupferron
a reasonable mimic of the transition state and/or intermediate that chelates the active site divalent metal ion and is bound in a conformation with the phenyl ring coplanar with the diazeniumdiolate moiety, active site binding, structure comparison with bound benzohydroxamate, overview
DL-alpha-Phenylglycidate
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binds at the active site of the enzyme, complete and irreversible inhibition in presence of Mg2+. Both D- and L-mandelate protect from inactivation
EDTA
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activity is fully restored upon addition of certain divalent metal ions. Mg2+ is the most effective, followed by Co2+, Ni2+, Mn2+ and Fe2+
