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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

Reaction

GTP
+
H2O
=
GDP
 +
phosphate

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 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.5 Acting on GTP to facilitate cellular and subcellular movement
                3.6.5.3 protein-synthesizing GTPase

Temperature Stability

Temperature Stability on EC 3.6.5.3 - protein-synthesizing GTPase

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105
the enzyme isoform EF-1beta retains 50% activity after 30 min at 105°C
20 - 100
-
EF-1alpha denaturation profile at pH 4.0, the protonation state of the numerous Asp and Glu residues plays a critical role for the thermally denatured state of the enzyme, reversibility of the inter-conversion between the two denatured forms, overview
40
about, melting point, recombinant enzyme
87 - 96
-
half-inactivation time 99 min at 87°C, half-inactivation time 3.5 min at 96°C
91
-
10 min, 50% inactivation of GDP binding ability, mutant enzyme G13A
92
-
half-denaturation of wild-type enzyme
93.6
-
temperature for half denaturation of D60A mutant
94
-
10 min, 50% inactivation of GDP binding ability, wild-type enzyme
95
-
10 min, 50% inactivation
95.1
-
temperature for half denaturation
96
-
binding of guanosine 5'-tetraphosphate to SsEF-1alpha renders the elongation factor more resistant to heat treatment. The denaturation profile of the elongation factor in the presence of guanosine tetraphosphate is shifted towards higher temperatures with a denaturation midpoint (96.4°C) about 2°C higher with respect to that observed for the elongation factor bound to GDP
additional information