|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
Enzymes and Genes:
acid phosphatase: appA
P-loop guanosine triphosphatase: yjiA
zinc-binding GTPase: yeiR
accessory protein for nickel incorporation into hydrogenase isoenzymes: hypB
selenocysteyl-tRNA-specific translation elongation factor: selB
50S ribosomal subunit stability factor: der
GTPase associated with the 50S subunit of the ribosome: hflX
ribosome small subunit-dependent GTPase A: rsgA
GTPase that interacts with methylmalonyl-CoA mutase: argK
Supersedes EC numbers: 188.8.131.52, 184.108.40.206, 220.127.116.11, 18.104.22.168, 22.214.171.124, 126.96.36.199
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name for 188.8.131.52: nucleoside-triphosphate phosphatase
Enzyme Commission Synonyms for 184.108.40.206: nucleoside-triphosphatase, nucleoside triphosphate phosphohydrolase, nucleoside-5-triphosphate phosphohydrolase, nucleoside 5-triphosphatase, unspecific diphosphate phosphohydrolase
Enzyme Commission Primary Name for 220.127.116.11: heterotrimeric G-protein GTPase
Enzyme Commission Primary Name for 18.104.22.168: small monomeric GTPase
Enzyme Commission Primary Name for 22.214.171.124: protein-synthesizing GTPase
Enzyme Commission Synonyms for 126.96.36.199: elongation factor (EF), initiation factor (IF), peptide-release or termination factor
Enzyme Commission Primary Name for 188.8.131.52: signal-recognition-particle GTPase
Enzyme Commission Primary Name for 184.108.40.206: dynamin GTPase
Enzyme Commission Primary Name for 220.127.116.11: tubulin GTPase
Enzyme Commission Summary for 18.104.22.168:
Also hydrolyses other nucleoside triphosphates, diphosphates, thiamine diphosphate and FAD.
Enzyme Commission Summary for 22.214.171.124:
This group comprises GTP-hydrolyzing systems, where GTP and GDP alternate in binding. This group includes stimulatory and inhibitory G-proteins such as Gs, Gi, Go and Golf, targetting adenylate cyclase and/or K+ and Ca2+ channels; Gq stimulating phospholipase C; transducin activating cGMP phosphodiesterase; gustducin activating cAMP phosphodiesterase. Golf is instrumental in odour perception, transducin in vision and gustducin in taste recognition. At least 16 different α subunits (39-52 kDa), 5 β subunits (36 kDa) and 12 γ subunits (6-9 kDa) are known.
Enzyme Commission Summary for 126.96.36.199:
A family of about 50 enzymes with a molecular mass of 21 kDa that are distantly related to the α-subunit of EC 188.8.131.52, heterotrimeric G-protein GTPase. 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).
Enzyme Commission Summary for 184.108.40.206:
This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis. In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyses it in prokaryotes. In eukaryotes, it is eIF-2 (150 kDa) that binds GTP. In the elongation phase, the GTP-hydrolysing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1α (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa). EF-Tu and EF-1α catalyse binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyse the translocation of peptidyl-tRNA from the A-site to the P-site. GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs.
Enzyme Commission Summary for 220.127.116.11:
Activity is associated with the signal-recognition particle (a protein- and RNA-containing structure involved in endoplasmic-reticulum-associated protein synthesis).
Enzyme Commission Summary for 18.104.22.168:
An enzyme with a molecular mass of about 100 kDa that is involved in endocytosis and is instrumental in pinching off membrane vesicles [Warnock96, McClure, Oh98].
Citations: [Matsushita68, Lewis65, Brightwell68, Tong93, Hsieh96, Klinger03, Placzek07, Neer95, Sprang97, Bondarenko97, Ming98, Bourne91, Hall94, Geyer97, Vitale98, Krab98, Kurzchalia84, Kisselev, Rodnina97, Freistroffer97, Connolly91 , Connolly89, Smets76, Miller93, Freymann97]
Relationship Links: BRENDA:EC:22.214.171.124, BRENDA:EC:126.96.36.199, BRENDA:EC:188.8.131.52, BRENDA:EC:184.108.40.206, BRENDA:EC:220.127.116.11, BRENDA:EC:18.104.22.168, BRENDA:EC:22.214.171.124, ENZYME:EC:126.96.36.199, ENZYME:EC:188.8.131.52, ENZYME:EC:184.108.40.206, ENZYME:EC:220.127.116.11, ENZYME:EC:18.104.22.168, ENZYME:EC:22.214.171.124, ENZYME:EC:126.96.36.199, IUBMB-ExplorEnz:EC:188.8.131.52, IUBMB-ExplorEnz:EC:184.108.40.206, IUBMB-ExplorEnz:EC:220.127.116.11, IUBMB-ExplorEnz:EC:18.104.22.168, IUBMB-ExplorEnz:EC:22.214.171.124, IUBMB-ExplorEnz:EC:126.96.36.199, IUBMB-ExplorEnz:EC:188.8.131.52
Bondarenko97: Bondarenko VA, Desai M, Dua S, Yamazaki M, Amin RH, Yousif KK, Kinumi T, Ohashi M, Komori N, Matsumoto H, Jackson KW, Hayashi F, Usukura J, Lipkin VM, Yamazaki A (1997). "Residues within the polycationic region of cGMP phosphodiesterase gamma subunit crucial for the interaction with transducin alpha subunit. Identification by endogenous ADP-ribosylation and site-directed mutagenesis." J Biol Chem 272(25);15856-64. PMID: 9188484
Connolly89: Connolly T, Gilmore R (1989). "The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide." Cell 57(4);599-610. PMID: 2541918
Freistroffer97: Freistroffer DV, Pavlov MY, MacDougall J, Buckingham RH, Ehrenberg M (1997). "Release factor RF3 in E.coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner." EMBO J 16(13);4126-33. PMID: 9233821
Geyer97: Geyer M, Wittinghofer A (1997). "GEFs, GAPs, GDIs and effectors: taking a closer (3D) look at the regulation of Ras-related GTP-binding proteins." Curr Opin Struct Biol 7(6);786-92. PMID: 9434896
Hsieh96: Hsieh HL, Tong CG, Thomas C, Roux SJ (1996). "Light-modulated abundance of an mRNA encoding a calmodulin-regulated, chromatin-associated NTPase in pea." Plant Mol Biol 30(1);135-47. PMID: 8616230
Miller93: Miller JD, Wilhelm H, Gierasch L, Gilmore R, Walter P (1993). "GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation." Nature 366(6453);351-4. PMID: 8247130
Ming98: Ming D, Ruiz-Avila L, Margolskee RF (1998). "Characterization and solubilization of bitter-responsive receptors that couple to gustducin." Proc Natl Acad Sci U S A 95(15);8933-8. PMID: 9671782
Oh98: Oh P, McIntosh DP, Schnitzer JE (1998). "Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium." J Cell Biol 141(1);101-14. PMID: 9531551
Roychowdhury99: Roychowdhury S, Panda D, Wilson L, Rasenick MM (1999). "G protein alpha subunits activate tubulin GTPase and modulate microtubule polymerization dynamics." J Biol Chem 274(19);13485-90. PMID: 10224115
Smets76: Smets LA, van Beek WP, van Rooij H (1976). "Surface glycoproteins and concanavalin-A-mediated agglutinability of clonal variants and tumour cells derived from SV40-virus-transformed mouse 3T3 cells." Int J Cancer 18(4);462-8. PMID: 185157
Tian99: Tian G, Bhamidipati A, Cowan NJ, Lewis SA (1999). "Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the alpha/beta-tubulin heterodimer." J Biol Chem 274(34);24054-8. PMID: 10446175
Tong93: Tong CG, Dauwalder M, Clawson GA, Hatem CL, Roux SJ (1993). "The major nucleoside triphosphatase in pea (Pisum sativum L.) nuclei and in rat liver nuclei share common epitopes also present in nuclear lamins." Plant Physiol 101(3);1005-11. PMID: 7508630
Vitale98: Vitale N, Moss J, Vaughan M (1998). "Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1)." J Biol Chem 273(5);2553-60. PMID: 9446556
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