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)
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.
History
EC 3.6.5.6 created 2000 as EC 3.6.1.51, transferred 2003 to EC 3.6.5.6
Reference
1  [PMID:9312004]
  Authors
Yu XC, Margolin W.
  Title
Ca2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro.
  Journal
EMBO J 16:5455-63 (1997)
DOI:10.1093/emboj/16.17.5455
Reference
2  [PMID:10446175]
  Authors
Tian G, Bhamidipati A, Cowan NJ, Lewis SA.
  Title
Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the alpha/beta-tubulin heterodimer.
  Journal
J Biol Chem 274:24054-8 (1999)
DOI:10.1074/jbc.274.34.24054
Reference
3  [PMID:10224115]
  Authors
Roychowdhury S, Panda D, Wilson L, Rasenick MM.
  Title
G protein alpha subunits activate tubulin GTPase and modulate microtubule polymerization dynamics.
  Journal
J Biol Chem 274:13485-90 (1999)
DOI:10.1074/jbc.274.19.13485
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