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4.1.1.33: diphosphomevalonate decarboxylase

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

Word Map on EC 4.1.1.33

Reaction

ATP
+
(R)-5-diphosphomevalonate
=
ADP
 +
phosphate
 +
isopentenyl diphosphate
 +
CO2

Synonyms

5-Pyrophosphomevalonate decarboxylase, Decarboxylase, pyrophosphomevalonate, diphosphomevalonate decarboxylase, diphosphomevalonte decarboxylase, DMD, DPM-DC, Fjoh_1389, MDD, MDP, Mevalonate (diphospho)decarboxylase, mevalonate 5'-diphosphate decarboxylase, Mevalonate 5-diphosphate decarboxylase, mevalonate diphosphate decarboxylase, mevalonate diphospho decarboxylase, Mevalonate pyrophosphate decarboxylase, mevalonate pyrophosphate decraboxylase, Mevalonate-5-pyrophosphate decarboxylase, More, MPD, MvaD, MVD, phosphomevalonate decarboxylase, PMD, Pyrophosphomevalonate decarboxylase, Pyrophosphomevalonic acid decarboxylase, ScMDD, ScMDD1, ScMDD2, scMVD, SSO2989

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.33 diphosphomevalonate decarboxylase

Crystallization

Crystallization on EC 4.1.1.33 - diphosphomevalonate decarboxylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapour diffusion method, with 0.1 M MES buffer pH 6.5, 20% PEG 5000 MME, 0.1 M NaCl, 1 mM dithiothreitol, and 0.2 M ammonium sulfate
purified enzyme in complex with (R)-5-diphosphomevalonate and adenosine 5'-O-(3-thio)triphosphate or with (R)-5-diphosphomevalonate and ADP, X-ray diffraction structure determination and analysis at 1.5-1.7 A resolution
hanging drop vapour diffusion method using 0.1 M Tris-HCl (pH 8.0), 1.8 M sodium malonate
molecular docking of inhibitors 6-fluoromevalonate diphosphate and diphosphoglycolylproline
-
hanging drop vapor diffusion method, using 0.25 M sodium formate and 16% (w/v) PEG 3350
MDD bound to diphosphoglycolyl proline and 6-fluoromevalonate diphosphate, hanging drop vapor diffusion method, using 0.25 M sodium formate and 16% (w/v) PEG 3350, at 20°C
molecular docking of inhibitor eriochrome black A, binds to the active site
wild-type and mutant S192A and D283A ternary complexes with inbhibitor 6-fluoromevalonate 5-diphosphate and ATPgammaS. During the catalytic mechanism, Asp283 correctly positions the mevalonate diphosphate acceptor substrate, while functioning as a catalytic base to abstract the acidic proton found on its C3-hydroxyl. This deprotonation facilitates an in-line transfer of the gamma-phosphoryl from the ATP donor. The Ser 107 side chain is appropriately positioned to hydrogen bond with both the beta- and gamma-phosphoryl groups of ATPgammaS within the ternary structure
in complex wih adenosine 5'-(beta,gamma-imido)-triphosphate and Mg2+
-