Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ATP | ATP interacts with FtsZDr and stimulates its GTPase activity by about 2fold possibly by increasing both substrate affinity and rate of reaction | Deinococcus radiodurans |
Cloned (Comment) | Organism |
---|---|
gene ftsZ or DR 0631, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) , FtsZDr-GFP expressing in Deinococcus radiodurans produces typical Z ring perpendicular to the plane of first cell division | Deinococcus radiodurans |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
EDTA | strong inhibition at 2 mM | Deinococcus radiodurans |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Deinococcus radiodurans |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | stimulates, can partially substitute for Mg2+ | Deinococcus radiodurans | |
Mg2+ | required, best metal cofactor, equirement of both Mg2+ and GTP for the polymerization of FtsZDr in higher ordered structure | Deinococcus radiodurans | |
Mn2+ | stimulates slightly, can partially substitute for Mg2+ | Deinococcus radiodurans | |
additional information | FtsZDr prefers Mg2+, followed by Co2+ for its GTPase activity. Mn2+ and Ni2+ support much lower GTPase activity, while GTP hydrolysis is nearly absent in the presence of Ca2+and Fe2+ | Deinococcus radiodurans | |
Ni2+ | stimulates slightly, can partially substitute for Mg2+ | Deinococcus radiodurans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
GTP + H2O | Deinococcus radiodurans | - |
GDP + phosphate | - |
? | |
additional information | Deinococcus radiodurans | enzyme FtsZDr acts as a GTPase exhibiting polymerization/depolymerization dynamics in vitro and FtsZ ring formation in vivo | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Deinococcus radiodurans | Q9RWN5 | gene ftsZ or DR 0631 | - |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by dialysis and nickel affinity chromatography, tag cleavage by thrombin, and dialysis | Deinococcus radiodurans |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
1.051 nmol phosphate/min/nmol FtsZ, purified recombinant enzyme, pH 7.5, 37°C | Deinococcus radiodurans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
GTP + H2O | - |
Deinococcus radiodurans | GDP + phosphate | - |
? | |
GTP + H2O | recombinant tubulin homologue FtsZDr binds to GTP and shows GTPase activity, equirement of both Mg2+ and GTP for the polymerization of FtsZDr in higher ordered structure. The critical concentrationof FtsZDr required for GTPase activity is 0.0001 mM | Deinococcus radiodurans | GDP + phosphate | - |
? | |
additional information | enzyme FtsZDr acts as a GTPase exhibiting polymerization/depolymerization dynamics in vitro and FtsZ ring formation in vivo | Deinococcus radiodurans | ? | - |
? | |
additional information | the enzyme produces bundles of protofilaments in the presence of either GTP or Mg2+ions. But the formation of the higher size ordered structures required both GTP and Mg2+in vitro. It shows polymerization/depolymerization dynamics as a function of GTP and Mg2+. Nucleotide binding studies with GTP and ATP, overview | Deinococcus radiodurans | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
FtsZ | - |
Deinococcus radiodurans |
FtsZDr | - |
Deinococcus radiodurans |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Deinococcus radiodurans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Deinococcus radiodurans |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme is involved in the mechanisms underlying regulation of cell division in response to DNA damage | Deinococcus radiodurans |
physiological function | FtsZDr, a tubulin homologue in radioresistant bacterium Deinococcus radiodurans, is characterized as a GTPase exhibiting polymerization/depolymerization dynamics in vitro and FtsZ ring formation in vivo | Deinococcus radiodurans |