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

BRENDA support

Literature summary for 2.7.4.2 extracted from

  • Huang, M.; Wei, K.; Li, X.; McClory, J.; Hu, G.; Zou, J.W.; Timson, D.
    Phosphorylation mechanism of phosphomevalonate kinase implications for rational engineering of isoprenoid biosynthetic pathway enzymes (2016), J. Phys. Chem. B, 120, 10714-10722 .
    View publication on PubMed
Search for more literature for 2.7.4.2

Protein Variants

Protein Variants Comment Organism
A293T site-directed mutagenesis, structure comparison with the wild-type enzyme Streptococcus pneumoniae
K101M site-directed mutagenesis, structure comparison with the wild-type enzyme Streptococcus pneumoniae
K101R site-directed mutagenesis, structure comparison with the wild-type enzyme Streptococcus pneumoniae
K9M site-directed mutagenesis, structure comparison with the wild-type enzyme Streptococcus pneumoniae
K9R site-directed mutagenesis, structure comparison with the wild-type enzyme Streptococcus pneumoniae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, Mg2+ is coordinated to the gamma-phosphoryl group of ATP in PMK Streptococcus pneumoniae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + (R)-5-phosphomevalonate Streptococcus pneumoniae
-
 ADP + (R)-5-diphosphomevalonate
-
 ?

Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate the phosphorylation reaction mechanism of phosphomevalonate kinase is studied by using molecular dynamics and hybrid QM/MM methods, overview. A conserved residue (Ser106) is reorientated to anchor ATP via a stable H-bond interaction. In addition, Ser213 located on the alpha-helix at the catalytic site is repositioned to further approach the substrate, facilitating the proton transfer during the phosphorylation. Lys101 functions to neutralize the negative charge developed at the beta-, gamma-bridging oxygen atom of ATP during phosphoryl transfer Streptococcus pneumoniae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + (R)-5-phosphomevalonate
-
 Streptococcus pneumoniae ADP + (R)-5-diphosphomevalonate
-
 ?
additional information ATP binding structue analysis Streptococcus pneumoniae ?
-
-

Subunits

Subunits Comment Organism
More Highly conserved motif II and p-loop in Streptococcus pneumoniae phosphomevalonate kinase, structure overview (PDB ID 3GON) Streptococcus pneumoniae

General Information

General Information Comment Organism
evolution the enzyme belongs to the the GHMP kinase superfamily Streptococcus pneumoniae
metabolism the enzyme is a representative kinase in the mevalonate pathway Streptococcus pneumoniae
additional information the phosphorylation reaction mechanism of phosphomevalonate kinase is studied by using molecular dynamics and hybrid QM/MM methods, the crystal structure of PMK in complex with its substrate (R)-5-phosphomevalonate (PMV) and AMPPNP-Mg2+ (PDB ID 3GON) is used as the initial structure. MD simulations are performed for the wild-type kinase and five variants, K9R, K9M, K101R, K101M, and A293T, respectively Streptococcus pneumoniae
physiological function distinct from other GHMP kinases, PMK catalyzes the transfer of the gamma-phosphate of ATP to another negatively charged phosphate in the substrate. In addition, Mg2+ is only coordinated to the gamma-phosphoryl group of ATP in PMK, whereas it is coordinated to at least two phosphoryl groups of ATP in other GHMP kinases, structure-function analysis, detailed overview Streptococcus pneumoniae