Cloned (Comment) | Organism |
---|---|
expression of His6-tagged maltose-binding-protein fusion HPPK in Escherichia coli strain BL21(DE3) | Yersinia pestis |
Crystallization (Comment) | Organism |
---|---|
purified recombinant HPPK in complex with 6-hydroxymethyl-7,8-dihydropterin and an ATP analogue AMPCPP, 8.0 mg/ml HPPK in 15 mM HP, 25 mM AMPCPP, 50 mM MgCl2 and 10 mM Tris-HCl, pH 8.0 s mixed with well solution containing 0.18 M ammonium acetate, 30% w/v PEG 4000, 20 mM imidazole, and 0.1 M sodium acetate, pH 4.6, 1-3 weeks, X-ray diffraction structure determination and analysis, molecular replacement | Yersinia pestis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic mechanism and thermodynamics, overview | Yersinia pestis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Yersinia pestis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 6-hydroxymethyl-7,8-dihydropterin | Yersinia pestis | - |
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate | - |
? | |
additional information | Yersinia pestis | HPPK is a key enzyme in the folate-biosynthetic pathway and is essential for microorganisms but absent from mammals | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Yersinia pestis | Q7CKD7 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 6-hydroxymethyl-7,8-dihydropterin | - |
Yersinia pestis | AMP + (7,8-dihydropterin-6-yl)methyl diphosphate | - |
? | |
additional information | HPPK is a key enzyme in the folate-biosynthetic pathway and is essential for microorganisms but absent from mammals | Yersinia pestis | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | Arg79 and Gln88 may help to stabilize the homodimer. The long side chain of Arg79 in YpHPPK forms many hydrophobic interactions with Trp90 and Gln49 from the partner subunit and a weak hydrogen bond with the side chain of Gln49, which may help to stabilize the dimeric molecule | Yersinia pestis |
Synonyms | Comment | Organism |
---|---|---|
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase | - |
Yersinia pestis |
HPPK | - |
Yersinia pestis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.3 | - |
assay at | Yersinia pestis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Yersinia pestis |