KEGG   ENZYME: 3.6.5.6Help
Entry
EC 3.6.5.6                  Enzyme                                 

Name tubulin GTPase
Class Hydrolases;
Acting on acid anhydrides;
Acting on GTP to facilitate cellular and subcellular movement
BRITE hierarchy
Sysname GTP phosphohydrolase (microtubule-releasing)
Reaction(IUBMB) GTP + H2O = GDP + phosphate [RN:R00335]
Reaction(KEGG) R00335
Show
Substrate GTP [CPD:C00044];
H2O [CPD:C00001]
Product GDP [CPD:C00035];
phosphate [CPD:C00009]
Comment An intrinsic activity of alpha-tubulin involved in tubulin folding,
division plane formation in prokaryotic cells and others.
Reference
  Authors
  Title

  Journal
  Organism
1  [PMID:9312004]
Yu XC, Margolin W.
Ca2+-mediated GTP-dependent dynamic assembly of bacterial cell
division protein FtsZ into asters and polymer networks in vitro.
EMBO. J. 16 (1997) 5455-63.
Escherichia coli [GN:eco]
Reference
  Authors
  Title

  Journal
  Organism
2  [PMID:10446175]
Tian G, Bhamidipati A, Cowan NJ, Lewis SA.
Tubulin folding cofactors as GTPase-activating proteins. GTP
hydrolysis and the assembly of the alpha/beta-tubulin heterodimer.
J. Biol. Chem. 274 (1999) 24054-8.
Bos taurus [GN:bta], Mus musculus [GN:mmu]
Reference
  Authors
  Title

  Journal
  Organism
3  [PMID:10224115]
Roychowdhury S, Panda D, Wilson L, Rasenick MM.
G protein alpha subunits activate tubulin GTPase and modulate
microtubule polymerization dynamics.
J. Biol. Chem. 274 (1999) 13485-90.
Bos taurus [GN:bta], Ovis aries
Other DBs ExplorEnz - The Enzyme Database: 3.6.5.6
IUBMB Enzyme Nomenclature: 3.6.5.6
ExPASy - ENZYME nomenclature database: 3.6.5.6
BRENDA, the Enzyme Database: 3.6.5.6

DBGET integrated database retrieval system