3.6.5.3: protein-synthesizing GTPase
This is an abbreviated version!
For detailed information about protein-synthesizing GTPase, go to the full flat file.
Word Map on EC 3.6.5.3
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3.6.5.3
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gtpases
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eif4e
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spacer
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ras
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actin
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rapamycin
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1-alpha
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gdp
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aminoacyl-trnas
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mtor
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rrna
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perk
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clade
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fusarium
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potato
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conidia
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chop
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reticulocyte
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dextrose
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polysomes
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rna-dependent
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gtp-binding
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aminoacylated
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cap-dependent
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adp-ribosylation
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pausing
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monophyletic
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oxysporum
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wilt
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cdc42
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beta-tubulin
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stall
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autophosphorylation
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normfinder
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atf6
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rinsed
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gdp-bound
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reisolated
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neurofibromatosis
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sh2
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preinitiation
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discolor
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interferon-induced
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anticodons
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p21ras
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genorm
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diphtheria
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rnapii
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hyaline
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caspase-12
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medicine
- 3.6.5.3
- gtpases
- eif4e
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spacer
- ras
- actin
- rapamycin
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1-alpha
- gdp
- aminoacyl-trnas
- mtor
- rrna
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perk
- clade
- fusarium
- potato
- conidia
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chop
- reticulocyte
- dextrose
- polysomes
-
rna-dependent
-
gtp-binding
-
aminoacylated
-
cap-dependent
-
adp-ribosylation
-
pausing
-
monophyletic
- oxysporum
-
wilt
- cdc42
- beta-tubulin
-
stall
- autophosphorylation
-
normfinder
- atf6
-
rinsed
-
gdp-bound
-
reisolated
- neurofibromatosis
- sh2
-
preinitiation
-
discolor
-
interferon-induced
-
anticodons
-
p21ras
-
genorm
- diphtheria
- rnapii
-
hyaline
- caspase-12
- medicine
Reaction
Synonyms
50S ribosomal subunit assembly factor, aEF-1alpha, aIF2, aIF2 GTPase, aIF2-gamma, aIF2B, aIF2gamma, aIF5B, archaeal initiation factor 2, archaeal initiation factor 2C, archaeal translation initiation factor 2, BipA, BPI-inducible protein A, Bst-IF2, chloroplast elongation factor G, EC 3.6.1.48, Ec-L10, Ec-L11, Ec-L12, Eco-IF2, eEF1A, eEF2, EF 1 alpha, EF-1alpha, EF-1beta, EF-2, EF-4, EF-G, EF-G GTPase, EF-G1, EF-G1mt, EF-like GTPase, EF-Tu, EF-Tumt, EF4, EFL, Efl1, Efl1 GTPase, eIEF2, eIF 2, eIF2, eIF2A, eIF2alpha, eIF2B, eIF5, eIF5B, elongation factor, elongation factor (EF), elongation factor 1 alpha, elongation factor 1alpha, elongation factor 2, elongation factor 4, elongation factor G, elongation factor thermo unstable, elongation factor Tu, elongation factor-1alpha, elongation factor-1beta, elongation factor-2, elongation factor-like 1, elongation factor-like 1 GTPase, eukaryotic elongation factor 2, eukaryotic elongation factor one alpha, eukaryotic initiation factor 2, eukaryotic initiation factor 2A, eukaryotic initiation factor 5B, eukaryotic translation initiation factor 2, eukaryotic translation initiation factor 5B, fusA, GTP phosphohydrolase, GTPase, GTPase aIF5B, GTPase HflX, GTPase-activating protein, guanine triphosphatase, guanine-nucleotide-exchange factor of eIF2, guanosine 5'-triphosphatase, guanosine triphosphatase, HflX, HflX GTPase, IF-2, IF1, IF2, IF2 GTPase, IF2alpha, IF3, IF5B, infB, initiation factor (IF), initiation factor 2, initiation factor 3, initiation factor 5B, initiation factor aIF5B, initiation factor-2, L10, L11, L12, LepA, mitochondrial elongation factor G, mitochondrial initiation factor 2, peptide-release or termination factor, protein-synthesizing GTPase, protein-sythesizing GTPase, RF3, ribosomal GTPase, ribosome-bound initiation factor 2, ribosome-dependent GTPase, SelB, selenocysteine tRNA-specific elongation factor, signal recognition particle GTPase Ffh, SRP GTPase Ffh, Ss-aIF2, SsEF-1alpha, SsEF-2, SsGBP, SSO0269, SSO0412, SSO1050, SSO2381, SsoHflX, translation elongation factor 2, translation factor aIF2/5B, translation initiation factor, translation initiation factor 2, translation initiation factor 2 gamma, translation initiation factor 5B, translation initiation factor eIF5, translation initiation factor IF1, translation initiation factor IF2, translation termination factor eRF3, translational GTPase, translational guanosine triphosphatase, translational initiation factor 2, trGTPase, Tt-L11, ymIF2
ECTree
3.6.5.3 protein-synthesizing GTPaseAdvanced search results
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results (Activating Compound
Activating Compound on EC 3.6.5.3 - protein-synthesizing GTPase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
1-propanol
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stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
2-propanol
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stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
eIF1A
GTPase-activating protein (GAP) for eIF2, the interaction is mediated by an eIF5B-binding motif located at the C-terminus of eIF1A. The C-terminal tail of eIF1A is located in the ribosomal P-site and counteracts the transition from open to closed complex. EIF5 competes with eIF1A for binding to eIF5B
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ethanol
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stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
glycerol
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stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
GMP-PCP
non-hydrolyzable or slowly hydrolyzable GTP analogues such as GMP-PCP and GMP-PNP, able to stall elongation factor on the ribosome, increase the efficiency of the reverse translocation reaction
GMP-PNP
non-hydrolyzable or slowly hydrolyzable GTP analogues such as GMP-PCP and GMP-PNP, able to stall elongation factor on the ribosome, increase the efficiency of the reverse translocation reaction
methanol
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stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
pulvomycin
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increasing pulvomycin concentration increased the rate of the intrinsic GTPase catalysed by elongation factor 1alpha, reaching its maximum stimulation effect at 30 mM. Pulvomycin exerts its stimulatory function at all the tested temperatures (45-75°C).
eIF5
eIF5 is the GTPase-activating protein (GAP) of eIF2, eIF5 promotes GTP hydrolysis by eIF2, followed by phosphate release. EIF2-GDP has lower affinity for Met-tRNAi than eIF2-GTP, and is released together with its GAP, eIF5
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eIF5
human eIF5, the GTPase-activating protein (GAP) for eIF2, also binds to eIF5B, with affinity that is about two orders of magnitude higher than that of eIF1A. The interaction is mediated by an eIF5B-binding motif located at the C-terminus of eIF5, similar to that of eIF1A and the two proteins compete for binding to eIF5B. NMR structure analysis of the binding interface between eIF5-CT39 and eIF5B-D4, structure of the human eIF5B-D4-eIF5-C-terminal tail (CTT) complex, overview
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kirromycin
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enhances activity of mutant enzyme G13A (maximal stimulation at 0.04 mM), does not stimulate intrinsic GTPase of SsEF-1alpha triggered by 3.6 M NaCl
L7/12
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functional compatibility between elongation factor G and the L7/12 protein in the ribosome governs its translational specificity
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L7/12
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the C-terminal domian of L7/12 is responsible for EF-Tu function. Functional compatibility between elongation factor Tu and the L7/12 protein in the ribosome governs its translational specificity
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NaCl
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intrinsic GTPase activity of elongation factor 1alpha is triggered in vitro by NaCl at molar concentrations. The sodium ion is responsible for the induction of the GTPase activity, whereas the anion modulates the enzymatic activity through destabilization of particular regions of the protein
NaCl
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intrinsic GTPase activity that is triggered in vitro by NaCl at molar concentrations
ribosome
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stimulates GTPase activity of elongation factor Tu. The factor binding site is loacetd on the 50S ribosomal subunit and comprises proteins L7/12, L10, L11, the l11-binding region of 23 rRNA, and the sarcin-ricin loop of 23S rRNA. L7/12 stimulates the GTPase activity of elongation factor G by inducing the catalytically active conformation of the G domain
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ribosome
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stimulates GTPase activity of elongation factor Tu. The factor binding site is loacetd on the 50S ribosomal subunit and comprises proteins L7/12, L10, L11, the l11-binding region of 23 rRNA, and the sarcin-ricin loop of 23S rRNA. L7/12 stimulates the GTPase activity of elongation factor Tu by inducing the catalytically active conformation of the G domain
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additional information
activity triggered by ribosome-induced conformational changes of EF-Tu
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additional information
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activity triggered by ribosome-induced conformational changes of EF-Tu
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additional information
the 30S ribosome does not stimulate the enzyme
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additional information
conserved residue His91 plays a direct role in the switch II loop of EF-G in GTPase activation
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additional information
GTP hydrolysis by EF-G gets strongly stimulated by the ribosome
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additional information
the GTPase activity of LepA, like that of other translational GTPases, is stimulated by interactions with both subunits of the ribosome
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additional information
evolutionary conservation of the eIF5B-binding motif in eIF1A and eIF5
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additional information
P05198; P20042; P41091
evolutionary conservation of the eIF5B-binding motif in eIF1A and eIF5
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additional information
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evolutionary conservation of the eIF5B-binding motif in eIF1A and eIF5
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additional information
presence of nonhydrolyzable GTP analogues increases the reverse translocation at mRNA activity of eukaryotic elongation factor eEF2. Reverse translocation requires an excessive concentration of cognate deacylated tRNA
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additional information
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active in GTP-bound form, inactive in GDP-bound form
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additional information
active in GTP-bound form, inactive in GDP-bound form
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additional information
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GTP hydrolysis is essential for release of eIF5B from the 80S ribosomal subunit
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additional information
active in GTP-bound form, inactive in GDP-bound form
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additional information
active in GTP-bound form, inactive in GDP-bound form
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additional information
EF4 GTPase activation upon ribosome binding
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