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Literature summary for 2.7.4.8 extracted from
- Purification and characterization of guanylate kinase, a nucleoside monophosphate kinase of Brugia malayi (2014), Parasitology, 141, 1341-1352.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis, phylogenetic tree, recombinant expression of C-terminally and N-terminally His-tagged enzyme in Escherichia coli BL21 (DE3) | Brugia malayi |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| aurin | 82% inhibition at 0.05 mM | Brugia malayi |  |
| Ca2+ | high inhibition at 1 mM | Brugia malayi | |
| EDTA | complete inhibition at 1 mM | Brugia malayi | |
| additional information | no or poor inhibition by sulfhydryl group inhibitors p-chloromercuribenzoate and N-ethylmaleimide, reducing agents (DTT and BME) and His modification by diethyl dicarbonate. No or poor inhibition by DEC, ivermectin and levamisole | Brugia malayi | |
| Ni2+ | high inhibition at 1 mM | Brugia malayi | |
| PMSF | inhibits 65% at 5 mM | Brugia malayi | |
| suramin | 83.5% inhibition at 0.01 mM | Brugia malayi | |
| Zn2+ | high inhibition at 1 mM | Brugia malayi | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.03 | - |
GMP | pH 7.5, 25°C, recombinant enzyme | Brugia malayi | |
| 0.038 | - |
dGMP | pH 7.5, 25°C, recombinant enzyme | Brugia malayi | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Brugia malayi | |
| Mn2+ | can partially substitute for Mg2+ | Brugia malayi | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 24000 | - |
- |
Brugia malayi |
| 45000 | - |
gel filtration | Brugia malayi |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + GMP | Brugia malayi | - |
ADP + GDP | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Brugia malayi | Q5GS56 | gene GMK | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli BL21 (DE3) by nickel affinity chromatography | Brugia malayi |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + GMP = ADP + GDP | sequential catalytic mechanism | Brugia malayi |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + dGMP | - |
Brugia malayi | ADP + dGDP | - |
r | |
| ATP + GMP | - |
Brugia malayi | ADP + GDP | - |
r | |
| ATP + GMP | GMP and ATP served as the most effective phosphate acceptor and donor, respectively | Brugia malayi | ADP + GDP | - |
r | |
| dATP + GMP | - |
Brugia malayi | dADP + GDP | - |
r | |
| GTP + dAMP | - |
Brugia malayi | GDP + dADP | - |
r | |
| additional information | recombinant enzyme BmGK utilizes both GMP and dGMP as substrates. No activity with dTMP, UMP, CMP, dCMP, IMP, XMP, CTP, UTP, and TTP | Brugia malayi | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 24000, SDS-PAGE, gel filtration and glutaraldehyde cross-linking | Brugia malayi |
| More | the secondary structure of BmGK consists of 45% alpha-helices, 18% beta-sheets, by circular dichrosim analysis | Brugia malayi |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ATP: GMP phosphotransferase | - |
Brugia malayi |
| BmGK | - |
Brugia malayi |
| guanosine monophosphate kinase | - |
Brugia malayi |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
- |
Brugia malayi |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 15 | 50 | activity range, profile overview | Brugia malayi |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 510 | - |
dGMP | pH 7.5, 25°C, recombinant enzyme | Brugia malayi | |
| 1500 | - |
GMP | pH 7.5, 25°C, recombinant enzyme | Brugia malayi | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
- |
Brugia malayi |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 8 | activity range, profile overview | Brugia malayi |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Brugia malayi | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | free Mg+2 (not complexed to ATP) and GTP play a regulatory role in catalysis of BmGK. The enzyme shows a higher catalytic efficiency compared to the human enzyme and shows ternary complex (BmGK-GMP-ATP) formation with sequential substrate binding. Homology modelling and docking study with GMP using the crystal structure of the yeast enzyme, PDB ID 1EX7 | Brugia malayi |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 13400 | - |
GMP | pH 7.5, 25°C, recombinant enzyme | Brugia malayi | |
| 50000 | - |
GMP | pH 7.5, 25°C, recombinant enzyme | Brugia malayi | |
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