3.6.5.6: tubulin GTPase
This is an abbreviated version!
For detailed information about tubulin GTPase, go to the full flat file.
Word Map on EC 3.6.5.6
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3.6.5.6
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polymerization
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actin
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cytoskeleton
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mitotic
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spindle
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microtubule-associated
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taxol
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centrosome
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paclitaxel
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nucleation
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tau
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disassembly
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antiproliferative
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heterodimers
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antimitotic
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nerve
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vinblastine
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interphase
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isotypes
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nocodazole
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microtubular
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neurite
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gtpases
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pole
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axonemal
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vimentin
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polymerized
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neurofilament
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kinesins
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cortical
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gdp
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cytokine
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cilia
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myosin
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dynein
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lattice
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metaphase
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map2
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microfilaments
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taxanes
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anaphase
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urchin
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multipolar
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catastrophe
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vincristine
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kinetochore
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microtubule-based
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nestin
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flagella
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docetaxel
- 3.6.5.6
- polymerization
- actin
- cytoskeleton
-
mitotic
- spindle
-
microtubule-associated
- taxol
- centrosome
- paclitaxel
-
nucleation
- tau
-
disassembly
-
antiproliferative
- heterodimers
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antimitotic
- nerve
- vinblastine
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interphase
-
isotypes
- nocodazole
- microtubular
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neurite
- gtpases
- pole
-
axonemal
- vimentin
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polymerized
- neurofilament
- kinesins
- cortical
- gdp
- cytokine
- cilia
- myosin
- dynein
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lattice
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metaphase
- map2
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microfilaments
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taxanes
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anaphase
- urchin
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multipolar
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catastrophe
- vincristine
- kinetochore
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microtubule-based
- nestin
- flagella
- docetaxel
Reaction
Synonyms
atypical GTPase, BtubB, cell division protein, EC 3.6.1.51, eFtsZ, FtsZ, FtsZ tubulin-like protein, FtsZDr, gamma-tubulin, GTP phosphohydrolase, GTPase, guanine triphosphatase, guanosine 5'-triphosphatase, guanosine triphosphatase, mFtsZ, ORF156, ribosomal GTPase, TUBG1, tubulin, tubulin FtsZ, tubulin GTPase, tubulin homolog FtsZ, tubulin-colchicine GTPase
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Substrates Products
Substrates Products on EC 3.6.5.6 - tubulin GTPase
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REACTION DIAGRAM
ATP + H2O
ADP + phosphate
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hydrolyzed at a rate about half as fast like GTP
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XTP + H2O
XDP + phosphate
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hydrolyzed at a rate about half as fast like GTP
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GTP + H2O
GDP + phosphate
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GTP + H2O
GDP + phosphate
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inverse isotope effect, reaction rate in D2O is twice the rate in H2O
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GTP + H2O
GDP + phosphate
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GTP-binding proteins from the tubulin family, including alpha,beta-tubulin are key components of the cytoskeleton and play central roles in chromosome segregation and cell division. The nucleotide switch of alpha,beta-tubulin is triggered by GTP hydrolysis and regulates microtubule assembly dynamics. Unassembled tubulin-GTP is in the inactive, curved conformation as in tubulin-GDP rings, and is driven into the straight microtubule conformation by the assembly contacts. Binding of the GTP gamma-phosphate only lowers the free energy difference between the curved and straight forms
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GTP + H2O
GDP + phosphate
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
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GTP + H2O
GDP + phosphate
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GTP-binding proteins from the tubulin family, including alpha,beta-tubulin are key components of the cytoskeleton and play central roles in chromosome segregation and cell division. The nucleotide switch of alpha,beta-tubulin is triggered by GTP hydrolysis and regulates microtubule assembly dynamics. Unassembled tubulin-GTP is in the inactive, curved conformation as in tubulin-GDP rings, and is driven into the straight microtubule conformation by the assembly contacts. Binding of the GTP gamma-phosphate only lowers the free energy difference between the curved and straight forms
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additional information
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enzyme FtsZDr acts as a GTPase exhibiting polymerization/depolymerization dynamics in vitro and FtsZ ring formation in vivo
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additional information
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enzyme FtsZDr acts as a GTPase exhibiting polymerization/depolymerization dynamics in vitro and FtsZ ring formation in vivo
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additional information
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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
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additional information
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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
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additional information
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the guanosine triphosphatase (GTPase) activity of FtsZ is highly conserved, and the binding and hydrolysis of GTP underlie the dynamic assembly and disassembly of FtsZ
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additional information
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the guanosine triphosphatase (GTPase) activity of FtsZ is highly conserved, and the binding and hydrolysis of GTP underlie the dynamic assembly and disassembly of FtsZ
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additional information
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GTP hydrolysis occurs at a single exchangeable GTP-binding site which is at the interface between head-to-tail arranged heterodimer enzyme
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additional information
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gamma-tubulin binds to mitochondrial DNA
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additional information
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GTP binding to the alpha occurs in the dimerization region between the alpha and beta monomers and remains unhydrolyzed. This is called the non-exchangeable site or N-site. GTP binding to beta-tubulin sits at the interface between two dimers within the protofilament, the longitudinal lattice of tubulin dimers running parallel to the microtubule filament long axis. Tubulin controls microtubule dynamics, analysis of GTP hydrolysis on reconstructed microtubules, mechanism, overview. GTP binding to the beta tubulin is hydrolyzable and this site is called the exchangeable site or E-site. Hydrolysis of GTP at the E-site is required for microtubule dynamic instability. GTP hydrolysis leads to the compaction of the lattice around the interdimer longitudinal interface sandwiching the E-site nucleotide. This compaction in turn results in a conformational rearrangement in all alpha-tubulin monomers corresponding to a small rotation of the intermediate domain and C-terminal H11-H12 helices with respect to the N-terminal domain in alpha-tubulin. Additionally, helix H8 from alpha-tubulin is also distorted in the GDP-state. The hydrolysis is immediate, but the probability of hydrolysis within a certain time is increased when the next dimer binds. Such catalysis leads to a situation where dimers at the end of the filament typically have GTP, and are in a non-compacted, straight conformation. This is called the GTP cap. Dimers within the body of the filament are typically in the GDP-state and prefer to be in the compacted, bent conformation. Due to binding to neighbors, the GDP dimers cannot compact and are held straight. Thus, GDP dimers in the body are in a high potential energy state, spring-loaded to compact whenever constraints are relaxed. The purpose of the GTPase is to force dimers within the body into this spring-loaded state. When the dimers at the top are lost or hydrolyzed stochastically, the end cap loses coherence and the entire microtubule bends back to relax the dimers to their lowest energy state. The longitudinal binding is less affected by the hydrolysis and protofilaments peel back into rings unraveling the microtubule
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additional information
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efficiency of in vitro tubulin polymerization in solutions containing a non-hydrolyzable analogue of GTP, GpCpp, instead of GTP is much higher than that in the presence of GTP
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