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D19A
site-directed mutagenesis, the mutation does not strongly modify the GDP binding properties of the two mutant enzyme, but reduces the GTP hydrolysis rate
D19A/H97A
site-directed mutagenesis, almost inactive mutant
H97A
site-directed mutagenesis, the mutation does not strongly modify the GDP binding properties of the two mutant enzyme, but reduces the GTP hydrolysis rate
D60A
-
1.4fold slower hydrolysis of GTP
F236P
kcat/Km is 63% compared to wild-type value
G13A
-
compared to wild-type enzyme the mutant shows a reduced rate of Phe polymerization and a reduced intrinsic GTPase activity that is stimulated by high concentrations of NaCl. Mutant enzyme shows an increased affinity for GTP and GDP. The temperature inducing a 50% denaturation of the mutant enzyme is 5°C lower than that of the wild-type enzyme
G235P
complete loss of GTP hydrolyzing activity
G235S
partial loss of GTP hydrolyzing activity
N189P
complete loss of GTP hydrolyzing activity
Ss(G)EF-1alpha
-
truncated form of SsEF-1alpha
Ss(GM)EF-1alpha
-
truncated form of SsEF-1alpha
T193N
complete loss of GTP hydrolyzing activity
T213V
kcat is 45% compared to the wild-type value
Y54H
the mutant of isoform EF-1beta shows wild type activity
A26G
-
converts the guanine nucleotide binding consensus sequences A-X-X-X-X-G-K-[T,S] of the elongation factor EF-2 into the corresponding G-X-X-X-X-G-K-[T,S] motif which is present in all the other GTP-binding proteins. In the mutant, the rate of poly(U)-directed poly(Phe) synthesis and the ribosome-dependent GTPase activity of A26GSsEF-2 are decreased. A26G substitution enhances the catalytic efficiency of the intrinsic SsEF-2 GTPase triggered by ethylene glycol and decreases the affinity for GDP
A26G
the mutant of isoform EF-2 shows increased wild type activity
additional information
mutant gamma subunit structure determination and analysis, and comparison to the wild-type gamma subunit structure, GTP binding structures, overview
additional information
-
comparison of sequence with that of Sulfolobus solfataricus strain MT4 shows only one amino acid change, i.e. I15V. The difference is in the first guanine nucleotide binding consensus sequence G13HIDHGK and is responsible for a increased efficiency in protein synthesis, which is accompanied by an reduced affinity for both guanosine diphosphate (GDP) and guanosine triphosphate (GTP), and an decreased efficiency in the intrinsic GTPase activity. The exchange has only very marginal effects on the thermal properties of the enzyme
additional information
comparison of sequence with that of Sulfolobus solfataricus strain MT4 shows only one amino acid change, i.e. I15V. The difference is in the first guanine nucleotide binding consensus sequence G13HIDHGK and is responsible for a increased efficiency in protein synthesis, which is accompanied by an reduced affinity for both guanosine diphosphate (GDP) and guanosine triphosphate (GTP), and an decreased efficiency in the intrinsic GTPase activity. The exchange has only very marginal effects on the thermal properties of the enzyme
additional information
-
comparison of sequence with that of Sulfolobus solfataricus strain MT4 shows only one amino acid change, i.e. V15I. The difference is in the first guanine nucleotide binding consensus sequence G13HIDHGK and is responsible for a reduced efficiency in protein synthesis, which is accompanied by an increased affinity for both guanosine diphosphate (GDP) and guanosine triphosphate (GTP), and an increased efficiency in the intrinsic GTPase activity. The exchange has only very marginal effects on the thermal properties of the enzyme
additional information
comparison of sequence with that of Sulfolobus solfataricus strain MT4 shows only one amino acid change, i.e. V15I. The difference is in the first guanine nucleotide binding consensus sequence G13HIDHGK and is responsible for a reduced efficiency in protein synthesis, which is accompanied by an increased affinity for both guanosine diphosphate (GDP) and guanosine triphosphate (GTP), and an increased efficiency in the intrinsic GTPase activity. The exchange has only very marginal effects on the thermal properties of the enzyme
additional information
-
construction of truncated forms corresponding to the putative domains G+M, and domain G. Neither truncated form is able to sustain poly(Phe) synthesis but they are able to bind guanine nucleotides with an affinity much higher with respect to that of the intact factor. Kinetic data are not changed by the truncation, but both forms are less thermostable than the intact factor and both are no more sensitive to the stimulatory effect of elongation factor 1beta
additional information
the N-terminal deletion mutant displays a similar Km value as the wild-type enzyme whereas the substrate kcat is 24fold increased
additional information
-
the N-terminal deletion mutant displays a similar Km value as the wild-type enzyme whereas the substrate kcat is 24fold increased
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Saccharolobus solfataricus (Q980A5), Saccharolobus solfataricus
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Saccharolobus solfataricus, Saccharolobus solfataricus ATCC 49255
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Saccharolobus solfataricus (Q980A5), Saccharolobus solfataricus P2 (Q980A5), Saccharolobus solfataricus JCM 11322 (Q980A5), Saccharolobus solfataricus ATCC 35092 (Q980A5), Saccharolobus solfataricus DSM 1617 (Q980A5)
brenda