Tubulin GTPase
| Tubulin GTPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.5.6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Tubulin GTPase (EC 3.6.5.6) is an enzyme with systematic name GTP phosphohydrolase (microtubule-releasing).[1][2][3] This enzyme catalyses the following chemical reaction
- GTP + H2O GDP + phosphate
This enzyme participates in tubulin folding and division plane formation.
See also
[edit]References
[edit]- ^ Yu XC, Margolin W (September 1997). "Ca2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro". The EMBO Journal. 16 (17): 5455–63. doi:10.1093/emboj/16.17.5455. PMC 1170176. PMID 9312004.
- ^ Tian G, Bhamidipati A, Cowan NJ, Lewis SA (August 1999). "Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the alpha/beta-tubulin heterodimer". The Journal of Biological Chemistry. 274 (34): 24054–8. doi:10.1074/jbc.274.34.24054. PMID 10446175.
- ^ Roychowdhury S, Panda D, Wilson L, Rasenick MM (May 1999). "G protein alpha subunits activate tubulin GTPase and modulate microtubule polymerization dynamics". The Journal of Biological Chemistry. 274 (19): 13485–90. doi:10.1074/jbc.274.19.13485. PMID 10224115.
External links
[edit]- Tubulin+GTPase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
