EC Number   |
General Information |
Reference |
|---|
   3.6.5.6 | evolution |
tubulin comes as a heterodimer of alpha and beta forms While there is only 45% amino-acid sequence similarity between alpha and beta tubulin isoforms, the three-dimensional structures of the monomers are very similar, each consisting of three domains of similar length and secondary structure composition: the N-terminal, the middle, and the C-terminal domain. Both alpha and beta bind GTP |
756202 |
| 3.6.5.6 | malfunction |
enhancement of tubulin polymerization by Cl--induced blockade of intrinsic GTPase |
733253 |
| 3.6.5.6 | malfunction |
in FtsZ mutants with severely reduced treadmilling, the spatial distribution of septal synthesis and the molecular composition and ultrastructure of the septal cell wall are substantially altered. Z-ring dynamics are significantly reduced in mutants with lower GTPase activity. In addition, the subunit exchange rate constants (kex) of these mutants decreases with kcat in a manner consistent with coupling to GTP hydrolysis. FtsZ GTPase mutants change the spatial distribution pattern but not the rate of septal PG synthesis |
-, 758464 |
| 3.6.5.6 | malfunction |
reduced levels of gamma-tubulin or impairment of its GTPase domain disrupts the mitochondrial network and alters both their respiratory capacity and the expression of mitochondrial-related genes. By contrast, reduced mitochondrial number or increased protein levels of gamma-tubulin DNA-binding domain enhance the association of gamma-tubulin with mitochondria. Increased mitochondria protein transport and low cellular mitochondria content affect the gamma-tubulin meshwork. Sg-mediated knockdown of gamma-tubulin affects the activity of the mitochondria, but not the structure of the endoplasmic reticulum |
756504 |
| 3.6.5.6 | malfunction |
the buried mutation T238A in alphabeta-tubulin yields microtubules with dramatically reduced shrinking rate and catastrophe frequency, the mutation uncouples the tubulin conformational and GTPase cycles, revealing allosteric control of microtubule dynamics. The mutation causes these effects by suppressing a conformational change that normally occurs in response to GTP hydrolysis in the lattice, without detectably changing the conformation of unpolymerized alphabetab-tubulin. The mutation predominantly affects post-GTPase conformational and dynamic properties of microtubules, phenotype, overview |
733717 |
| 3.6.5.6 | metabolism |
gamma-tubulin forms a cellular meshwork of gamma-strings and gamma-tubules. While gamma-tubules are polar cytosolic filaments within the gamma-string meshwork, gamma-strings are detected in both the cytoplasm and the nucleus and are formed of non-polar protein threads that cross the double membrane of the nuclear envelope. The gamma-string meshwork forms a boundary around chromatin, which coordinates cytosolic and nuclear events during mitosis by assuring that a nuclear envelope forms around daughter chromosomes. The gamma-tubulin meshwork may be a dynamic network that contributes to cellular homeostasis |
756504 |
| 3.6.5.6 | metabolism |
microtubule dynamic instability depends on the GTPase activity of the polymerizing alphabeta-tubulin subunits, which cycle through at least three distinct conformations as they move into and out of microtubules. This conformational cycle contributes to microtubule growing, shrinking, and switching |
733717 |
| 3.6.5.6 | metabolism |
the enzyme is involved in the mechanisms underlying regulation of cell division in response to DNA damage |
733983 |
| 3.6.5.6 | more |
determination of Z-ring dynamics in live Escherichia coli strain BW25113 cells by using total internal reflection fluorescence (TIRF) microscopy to monitor the fluorescence of an FtsZ-GFP fusion protein. Mutants lacking one of the proteins that regulates the Z-ring (SlmA, SulA, MinC, ClpX, and ClpP) or stabilizes it (ZapA, ZapB, ZapC, ZapD, and MatP) also display wild-type Z-ring behavior. Thus, Z-ring dynamics are likely due to FtsZ's intrinsic polymerization properties, which are related to its GTPase activity. Z-ring dynamics were significantly reduced in mutants with lower GTPase activity |
-, 758464 |
| 3.6.5.6 | physiological function |
a part of stimulatory effects of Cl- on in vitro tubulin polymerization is mediated via an inhibitory effect on GTPase activity of tubulin, although Cl- also regulates in vitro tubulin polymerization by factors other than an inhibitory effect on GTPase activity |
733253 |
