Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Barta, M.L.; McWhorter, W.J.; Miziorko, H.M.; Geisbrecht, B.V.
    Structural basis for nucleotide binding and reaction catalysis in mevalonate diphosphate decarboxylase (2012), Biochemistry, 51, 5611-5621.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.33
-
Staphylococcus epidermidis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.33 hanging drop vapor diffusion method, using 0.25 M sodium formate and 16% (w/v) PEG 3350 Staphylococcus epidermidis
4.1.1.33 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 Staphylococcus epidermidis

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.33 D283A catalytically deficient enzyme with 100000fold decreased kcat value Staphylococcus epidermidis
4.1.1.33 D283A 10000fold decrease in kcat value Staphylococcus epidermidis
4.1.1.33 S192A catalytically deficient enzyme with 1000fold decreased kcat value Staphylococcus epidermidis
4.1.1.33 S192A 1000fold decrease in kcat value Staphylococcus epidermidis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.33 6-fluoromevalonate diphosphate competitive Staphylococcus epidermidis
4.1.1.33 diphosphoglycolyl-L-proline competitive Staphylococcus epidermidis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.33 Mg2+ required, bound to ATP Staphylococcus epidermidis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.33 ATP + (R)-5-diphosphomevalonate Staphylococcus epidermidis
-
ADP + phosphate + isopentenyl diphosphate + CO2
-
ir

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.33 Staphylococcus epidermidis Q9FD73
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.33
-
Staphylococcus epidermidis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.33 ATP + (R)-5-diphosphomevalonate
-
Staphylococcus epidermidis ADP + phosphate + isopentenyl diphosphate + CO2
-
ir

Synonyms

EC Number Synonyms Comment Organism
4.1.1.33 MDD
-
Staphylococcus epidermidis
4.1.1.33 mevalonate diphosphate decarboxylase
-
Staphylococcus epidermidis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.1.1.33 0.00005
-
diphosphoglycolyl-L-proline pH and temperature not specified in the publication Staphylococcus epidermidis
4.1.1.33 0.0043
-
6-fluoromevalonate diphosphate pH and temperature not specified in the publication Staphylococcus epidermidis