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

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

ECTree

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

General Stability

General Stability on EC 4.1.1.33 - diphosphomevalonate decarboxylase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is a multi-tryptophan protein, the tryptophan environment gets perturbed even at low concentrations of denaturant, and the unfolding is gradual and partially reversible. The secondary structure of MDD is quite stable in acidic as well as alkaline pH range
no requirement for SH-containing reagents for stability
-
stabilized by phenylmethylsulfonyl fluoride, aprotinin and leupeptin
-