Literature summary for 4.1.1.33 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.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Staphylococcus epidermidis

Crystallization (Commentary)

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

Crystallization (Comment)

Organism

hanging drop vapor diffusion method, using 0.25 M sodium formate and 16% (w/v) PEG 3350

Staphylococcus epidermidis

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

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

Inhibitors

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus epidermidis	Q9FD73	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Staphylococcus epidermidis

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
MDD	-	Staphylococcus epidermidis
mevalonate diphosphate decarboxylase	-	Staphylococcus epidermidis

Ki Value [mM]

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