Application | Comment | Organism |
---|---|---|
synthesis | potential of ZgHGPRT/AMPK as biocatalyst for the synthesis of nucleoside-50-mono-, di-, and triphosphates | Zobellia galactanivorans |
Cloned (Comment) | Organism |
---|---|
sequence comparisons, recombinant expression of N-terminally His6-tagged enzyme with a thrombin cleavage site in Escherichia coli strain BL21(DE3) | Zobellia galactanivorans |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Zobellia galactanivorans |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
soluble | - |
Zobellia galactanivorans | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | preferred metal ion | Zobellia galactanivorans | |
Mg2+ | preferred metal ion | Zobellia galactanivorans | |
additional information | the enzyme is dependent on divalent cations | Zobellia galactanivorans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate | Zobellia galactanivorans | - |
GMP + diphosphate | - |
? | |
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate | Zobellia galactanivorans CCUG 47099 | - |
GMP + diphosphate | - |
? | |
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate | Zobellia galactanivorans Dsij | - |
GMP + diphosphate | - |
? | |
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate | Zobellia galactanivorans DSM 12802 | - |
GMP + diphosphate | - |
? | |
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate | Zobellia galactanivorans CIP 106680 | - |
GMP + diphosphate | - |
? | |
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate | Zobellia galactanivorans NCIMB 13871 | - |
GMP + diphosphate | - |
? | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Zobellia galactanivorans | - |
IMP + diphosphate | - |
? | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Zobellia galactanivorans CCUG 47099 | - |
IMP + diphosphate | - |
? | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Zobellia galactanivorans Dsij | - |
IMP + diphosphate | - |
? | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Zobellia galactanivorans DSM 12802 | - |
IMP + diphosphate | - |
? | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Zobellia galactanivorans CIP 106680 | - |
IMP + diphosphate | - |
? | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Zobellia galactanivorans NCIMB 13871 | - |
IMP + diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Zobellia galactanivorans | G0LC40 | - |
- |
Zobellia galactanivorans CCUG 47099 | G0LC40 | - |
- |
Zobellia galactanivorans CIP 106680 | G0LC40 | - |
- |
Zobellia galactanivorans Dsij | G0LC40 | - |
- |
Zobellia galactanivorans DSM 12802 | G0LC40 | - |
- |
Zobellia galactanivorans NCIMB 13871 | G0LC40 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage through thrombin, and gel filtration | Zobellia galactanivorans |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.47 | - |
substrate guanosine, pH 8.0, 50°C, with 2.4 mM Mg2+ | Zobellia galactanivorans |
0.53 | - |
substrate hypoxanthine, pH 7.0, 50°C, with 2.4 mM Mg2+ | Zobellia galactanivorans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Zobellia galactanivorans | GMP + diphosphate | - |
? | |
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Zobellia galactanivorans CCUG 47099 | GMP + diphosphate | - |
? | |
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Zobellia galactanivorans Dsij | GMP + diphosphate | - |
? | |
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Zobellia galactanivorans DSM 12802 | GMP + diphosphate | - |
? | |
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Zobellia galactanivorans CIP 106680 | GMP + diphosphate | - |
? | |
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Zobellia galactanivorans NCIMB 13871 | GMP + diphosphate | - |
? | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Zobellia galactanivorans | IMP + diphosphate | - |
? | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Zobellia galactanivorans CCUG 47099 | IMP + diphosphate | - |
? | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Zobellia galactanivorans Dsij | IMP + diphosphate | - |
? | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Zobellia galactanivorans DSM 12802 | IMP + diphosphate | - |
? | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Zobellia galactanivorans CIP 106680 | IMP + diphosphate | - |
? | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Zobellia galactanivorans NCIMB 13871 | IMP + diphosphate | - |
? | |
additional information | ZgHGPRT/AMPK is a bifunctional enzyme, which acts as phosphoribosyltransferase or adenylate kinase depending upon the nature of the substrate. Substrate specificity, overview | Zobellia galactanivorans | ? | - |
- |
|
additional information | ZgHGPRT/AMPK is a bifunctional enzyme, which acts as phosphoribosyltransferase or adenylate kinase depending upon the nature of the substrate. Substrate specificity, overview | Zobellia galactanivorans CCUG 47099 | ? | - |
- |
|
additional information | ZgHGPRT/AMPK is a bifunctional enzyme, which acts as phosphoribosyltransferase or adenylate kinase depending upon the nature of the substrate. Substrate specificity, overview | Zobellia galactanivorans Dsij | ? | - |
- |
|
additional information | ZgHGPRT/AMPK is a bifunctional enzyme, which acts as phosphoribosyltransferase or adenylate kinase depending upon the nature of the substrate. Substrate specificity, overview | Zobellia galactanivorans DSM 12802 | ? | - |
- |
|
additional information | ZgHGPRT/AMPK is a bifunctional enzyme, which acts as phosphoribosyltransferase or adenylate kinase depending upon the nature of the substrate. Substrate specificity, overview | Zobellia galactanivorans CIP 106680 | ? | - |
- |
|
additional information | ZgHGPRT/AMPK is a bifunctional enzyme, which acts as phosphoribosyltransferase or adenylate kinase depending upon the nature of the substrate. Substrate specificity, overview | Zobellia galactanivorans NCIMB 13871 | ? | - |
- |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 41650, sedimentation velocity and SDS-PAGE, 2 * 43770, sequence caluclation | Zobellia galactanivorans |
More | quaternary structure analysis | Zobellia galactanivorans |
Synonyms | Comment | Organism |
---|---|---|
hypoxanthine-guanine phosphoribosyltransferase/adenylate kinase | - |
Zobellia galactanivorans |
More | cf. EC 2.7.4.3 | Zobellia galactanivorans |
ZgHGPRT/AMPK | - |
Zobellia galactanivorans |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | 60 | - |
Zobellia galactanivorans |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 80 | ZgHGPRT/AMPK displays over 70% of maximal activity across the broad temperature range of 30-80°C, with a maximum at 50-60°C | Zobellia galactanivorans |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | 45 | purified recombinant ZgHGPRT/AMPK exhibits an apparent unfolding temperature (Tm) of 45°C and a retained activity of around 80% when incubated at 40°C for 240 min | Zobellia galactanivorans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
- |
Zobellia galactanivorans |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 7 | ZgHGPRT/AMPK displays high activity in a narrow pH range 6.0-7.0, with a maximum peak in 50 mM sodium phosphate at pH 7.0 | Zobellia galactanivorans |
General Information | Comment | Organism |
---|---|---|
evolution | adenylate kinase (EC 2.7.4.3, AMPK) belongs to nucleoside-5'-monophosphate kinase (NMPK) family. ZgHGPRT/AMPK belongs to class I PRTs, which display a conserved 13-residue fingerprint region (PRPP binding-motif) in their amino acid sequence | Zobellia galactanivorans |
additional information | identification of a putative dual-domain hypoxanthine-guanine phosphoribosyltransferase (HGPRT)/adenylate kinase (AMPK). ZgHGPRT/AMPK single domain, dual domain 3D structure homology modeling, HGPRT from Leptospira interrogans (PDB ID 4QRI) and AMPK structure from Geobacillus stearothermophilus (PDB ID 1ZIN) are used as templates. ZgHGPRT/AMPK model is complexed with Hyp, PRPP and Mg2+ in the active site of the HGPRT domain, and with AMP, ATP and Mg2+ in the active site of AMPK domain. Essential elements of type I PRTs architecture are found in ZgHGPRT/AMPK amino acid sequence such as diphosphate loop, the flexible loop and PRPP binding domain (including PRPP loop), as well as in the homology model | Zobellia galactanivorans |
physiological function | the Zobellia galactanivorans enzyme contains both HGPRT (N-terminal part) and AMPK (C-terminal part) domains. The N-terminal HGPRT module is involved in the purine salvage and converts hypoxanthine to inosine-5'-monophosphate (IMP) and guanine to guanosine-5'-monophosphate (GMP) | Zobellia galactanivorans |