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Literature summary for 3.6.5.6 extracted from

  • Modi, K.M.; Tewari, R.; Misra, H.S.
    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 (2014), Int. J. Biochem. Cell Biol., 50, 38-46.
    View publication on PubMed

Activating Compound

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(Commentary)

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

Inhibitors Comment Organism Structure
EDTA strong inhibition at 2 mM Deinococcus radiodurans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Deinococcus radiodurans

Metals/Ions

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Deinococcus radiodurans Q9RWN5 gene ftsZ or DR 0631
-

Purification (Commentary)

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 [micromol/min/mg]

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 and Products (Substrate)

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

Synonyms Comment Organism
FtsZ
-
Deinococcus radiodurans
FtsZDr
-
Deinococcus radiodurans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Deinococcus radiodurans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Deinococcus radiodurans

General Information

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