KEGG   ENZYME: 3.6.5.2
Entry
EC 3.6.5.2                  Enzyme                                 
Name
small monomeric GTPase
Class
Hydrolases;
Acting on acid anhydrides;
Acting on GTP to facilitate cellular and subcellular movement
Sysname
GTP phosphohydrolase (cell-regulating)
Reaction(IUBMB)
GTP + H2O = GDP + phosphate [RN:R00335]
Reaction(KEGG)
R00335
Substrate
GTP [CPD:C00044];
H2O [CPD:C00001]
Product
GDP [CPD:C00035];
phosphate [CPD:C00009]
Comment
A family of about 50 enzymes with a molecular mass of 21 kDa that are distantly related to the alpha-subunit of heterotrimeric G-protein GTPase (EC 3.6.5.1). They are involved in cell-growth regulation (Ras subfamily), membrane vesicle traffic and uncoating (Rab and ARF subfamilies), nuclear protein import (Ran subfamily) and organization of the cytoskeleton (Rho and Rac subfamilies).
History
EC 3.6.5.2 created 2000 as EC 3.6.1.47, transferred 2003 to EC 3.6.5.2
Reference
1  [PMID:1898771]
  Authors
Bourne HR, Sanders DA, McCormick F.
  Title
The GTPase superfamily: conserved structure and molecular mechanism.
  Journal
Nature 349:117-27 (1991)
DOI:10.1038/349117a0
Reference
2  [PMID:7888179]
  Authors
Hall A.
  Title
Small GTP-binding proteins and the regulation of the actin cytoskeleton.
  Journal
Annu Rev Cell Biol 10:31-54 (1994)
DOI:10.1146/annurev.cb.10.110194.000335
Reference
3  [PMID:9434896]
  Authors
Geyer M, Wittinghofer A.
  Title
GEFs, GAPs, GDIs and effectors: taking a closer (3D) look at the regulation of Ras-related GTP-binding proteins.
  Journal
Curr Opin Struct Biol 7:786-92 (1997)
DOI:10.1016/S0959-440X(97)80147-9
Reference
4  [PMID:9446556]
  Authors
Vitale N, Moss J, Vaughan M.
  Title
Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1).
  Journal
J Biol Chem 273:2553-60 (1998)
DOI:10.1074/jbc.273.5.2553
Other DBs
ExplorEnz - The Enzyme Database: 3.6.5.2
IUBMB Enzyme Nomenclature: 3.6.5.2
ExPASy - ENZYME nomenclature database: 3.6.5.2
BRENDA, the Enzyme Database: 3.6.5.2

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