Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.6.5.6 - tubulin GTPase

for references in articles please use BRENDA:EC3.6.5.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
An intrinsic activity of alpha-tubulin involved in tubulin folding, division plane formation in prokaryotic cells and others.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: P23258
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
tubulin, gamma-tubulin, cell division protein, tubg1, tubulin homolog ftsz, tubulin gtpase, btubb, atypical gtpase, orf156, tubulin ftsz, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
gamma-tubulin
-
GTP phosphohydrolase
-
-
-
-
GTPase
-
-
-
-
guanine triphosphatase
-
-
-
-
guanosine 5'-triphosphatase
-
-
-
-
guanosine triphosphatase
-
-
-
-
ribosomal GTPase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoric ester hydrolysis
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
GTP phosphohydrolase (microtubule-releasing)
An intrinsic activity of alpha-tubulin involved in tubulin folding, division plane formation in prokaryotic cells and others.
CAS REGISTRY NUMBER
COMMENTARY hide
9059-32-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
calcium apparently competes for the magnesium binding site at the E-site to cause rapid hydrolysis of GTP to GDP
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
citral dimethyl acetal
CDA, impairs the GTPase activity of gamma-tubulin
Colchicine
a small molecule inhibitor that binds to tubulin dimers rendering them unable to incorporate into filaments. It does not destabilize actively, but rather inhibit repolymerization after regular depolymerization
vinblastine
a small molecule inhibitor that binds to tubulin dimers rendering them unable to incorporate into filaments. It does not destabilize actively, but rather inhibit repolymerization after regular depolymerization
additional information
a class of destabilizers consists of the microtubule-severing enzymes from the ATPases associated with various cellular activities (AAA+) family of ATP-enzymes. GTP-driven microtubule dynamics are coupled to ATP-driven destabilization by severing enzymes, examples and mechanism, detailed overview
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
tubulin gamma-1 chain
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
despite evidence that the mitochondrial proteome is derived from endosymbiotic bacteria, most mitochondria lack the expression of the gamma-tubulin homologue FtsZ, suggesting that gamma-tubulin may replace FtsZ function in mitochondria
Manually annotated by BRENDA team
nuclear localization signal (NLS) mediates gamma-tubulin translocation to the nucleus. The reduced import of gamma-tubulin to the nuclear compartment enhances the binding of gamma-tubulin to mtDNA
Manually annotated by BRENDA team
additional information
in close vicinity to the nuclear envelope, endogenous gamma-tubulin form a network of strings, gamma-strings, which grow from the nuclear compartment and towards the plasma membrane. Fixed U2OS cells transiently expressing gamma-tubulin sgRNA (Cas9-crispGFP) are immunofluorescence stained with an anti-MTCO2 antibody and a gamma-tubulin antibody originated in mouse. Nuclear localization signal (NLS) mediates gamma-tubulin translocation to the nucleus. The reduced import of gamma-tubulin to the nuclear compartment enhances the binding of gamma-tubulin to mtDNA
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
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
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TBG1_HUMAN
451
0
51170
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C13A
site-directed mutagenesis, mutation of Cyst13 to Ala (GFP-A13gamma-tubulinresist) impairs GTP binding to the GTPase domain, stable co-expresses of the mutated recombinant protein in gamma-tubulin sh-U2-OS cells
R399A/K400A/R409A
site-directed mutagenesis
additional information
generation of stably or transient transfected gamma-tubulin shRNA, pEGFP-gamma-tubulinresist, pEGFP-A13-gamma-tubulinresist, gamma-tubulinsgrest, gamma-tubulinR399A-K400A-R409A sgrest, and gamma-tubulin336-451 U2OS, and MCF10A cells. Stable co-expression of gamma-tubulin sgRNA depleting the endogenous gamma-tubulin pool. Fixed U2OS cells transiently expressing gamma-tubulin sgRNA (Cas9-crispGFP) are immunofluorescence stained with an anti-MTCO2 antibody and a gamma-tubulin antibody originated in mouse. Sg-mediated knockdown of gamma-tubulin affects the activity of the mitochondria, but not the structure of the endoplasmic reticulum
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
stable recombinant co-expression of the mutated C13A protein in gamma-tubulin sh-U2OS cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bailey, M.E.; Jiang, N.; Dima, R.I.; Ross, J.L.
Microtubule severing enzymes couple ATPase activity with tubulin GTPase spring loading
Biopolymers
105
547-556
2016
Homo sapiens (P23258)
Manually annotated by BRENDA team
Lindstroem, L.; Li, T.; Malycheva, D.; Kancharla, A.; Nilsson, H.; Vishnu, N.; Mulder, H.; Johansson, M.; Rossello, C.A.; Alvarado-Kristensson, M.
The GTPase domain of gamma-tubulin is required for normal mitochondrial function and spatial organization
Commun. Biol.
1
37
2018
Homo sapiens (P23258)
Manually annotated by BRENDA team