Crystallization (Comment) | Organism |
---|---|
the crystal structure is used for moelling with bound inhibitor tetramic acid | Micrococcus luteus |
Protein Variants | Comment | Organism |
---|---|---|
D26A | the mutant shows altered Mg2+ binding compared to the wild-type enzyme | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
BPH-629 | bindiing structure in enzyme chain B, overview | Escherichia coli | |
dihydropyridin-2-one | - |
Streptococcus pneumoniae | |
tetramic acid | the crystal structure is used for modelling with bound inhibitor tetramic acid | Micrococcus luteus | |
tetramic acid | binding structure, overview | Streptococcus pneumoniae | |
tetronic acid | - |
Streptococcus pneumoniae | |
Triton X-100 | C55 is retained in the active site for further elongation, whereas the kcat is increased by 190fold under steady-state condition by 0.1% Triton X-100 | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | pre-steady-state UPPS kinetics, single-turnover, kinetic analysis, overview | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required, structures of Mg2+ binding of wild-type and mutant UPPS, overview | Escherichia coli | |
Mg2+ | required, structures of Mg2+ binding of wild-type and mutant UPPS, overview | Micrococcus luteus | |
Mg2+ | required, structures of Mg2+ binding of wild-type and mutant UPPS, overview | Streptococcus pneumoniae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate | Micrococcus luteus | - |
8 diphosphate + ditrans,octacis-undecaprenyl diphosphate | - |
? | |
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate | Streptococcus pneumoniae | - |
8 diphosphate + ditrans,octacis-undecaprenyl diphosphate | - |
? | |
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate | Escherichia coli | UPPS catalyzes eight consecutive condensation steps of IPP with FPP to form C55 final product | 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate | - |
? | |
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate | Micrococcus luteus B-P 26 | - |
8 diphosphate + ditrans,octacis-undecaprenyl diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
gene uppS | - |
Micrococcus luteus | - |
gene uppS | - |
Micrococcus luteus B-P 26 | - |
gene uppS | - |
Streptococcus pneumoniae | Q97SR4 | gene uppS | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate | catalytic mechanism, overview | Escherichia coli | |
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate | catalytic mechanism, overview | Micrococcus luteus | |
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate | catalytic mechanism, overview | Streptococcus pneumoniae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate | - |
Escherichia coli | 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate | - |
? | |
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate | - |
Micrococcus luteus | 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate | - |
? | |
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate | - |
Streptococcus pneumoniae | 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate | - |
? | |
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate | UPPS catalyzes eight consecutive condensation steps of IPP with FPP to form C55 final product | Escherichia coli | 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate | - |
? | |
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate | - |
Micrococcus luteus B-P 26 | 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
undecaprenyl diphosphate synthase | - |
Escherichia coli |
undecaprenyl diphosphate synthase | - |
Micrococcus luteus |
undecaprenyl diphosphate synthase | - |
Streptococcus pneumoniae |
UPPs | - |
Escherichia coli |
UPPs | - |
Micrococcus luteus |
UPPs | - |
Streptococcus pneumoniae |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.0003 | - |
pH and temperature not specified in the publication | Streptococcus pneumoniae | tetramic acid | |
0.0006 | - |
pH and temperature not specified in the publication | Escherichia coli | BPH-629 |
General Information | Comment | Organism |
---|---|---|
physiological function | UPPS is a cis- and trans-type prenyltransferase catalyzing consecutive condensation reactions of FPP with specific numbers of IPP to generate linear products with designate chain lengths, UPPS utilizes a concerted mechanism for IPP condensation, structures and mechanisms of the cis-prenyltransferase undecaprenyl diphosphate synthase, overview. Structures of different forms of UPPS with or without ligands reveal conformational changes upon substrate binding, catalysis and product release. A disordered loop in Escherichia coli UPPS, invisible in crystal structures without ligand, is essential for catalysis | Escherichia coli |