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Information on EC 3.6.5.3 - protein-synthesizing GTPase

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EC Tree
IUBMB Comments
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-1alpha (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-1alpha 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.
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UNIPROT: P35021
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
elongation factor, translation initiation factor, gtpase-activating protein, eif2alpha, eif2b, elongation factor tu, eef1a, ef-1alpha, eukaryotic initiation factor 2, elongation factor g, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elongation factor 1alpha
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elongation factor-1alpha
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protein-sythesizing GTPase
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SsEF-1alpha
amino acid at position 15, strain MT3 valine, SsMT3EF-1alpha, strain MT4 isoleucine, SsMT4EF-1alpha
elongation factor (EF)
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GTP phosphohydrolase
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-
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GTPase
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-
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guanine triphosphatase
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-
-
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guanosine 5'-triphosphatase
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-
-
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guanosine triphosphatase
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-
-
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initiation factor (IF)
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-
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peptide-release or termination factor
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ribosomal GTPase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
GTP phosphohydrolase (mRNA-translation-assisting)
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-1alpha (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-1alpha 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.
CAS REGISTRY NUMBER
COMMENTARY hide
9059-32-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0009 - 0.0027
GTP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013 - 0.015
GTP
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.1
isoform EF-1alpha, calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
EF1A_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
435
0
48489
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 49000, isoform EF-1alpha, calculated from amino acid sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
87
the enzyme isoform EF-1alpha retains 54% activity after 6 h at 87°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
the gene encoding SsEF-1alpha from the strain MT3 is cloned, sequenced and expressed in Escherichia coli, the vectors pGEM-3Z and pET22 are used
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Masullo, M.; Cantiello, P.; Lamberti, A.; Longo, O.; Fiengo, A.; Arcari, P.
Cloning, expression and evolution of the gene encoding the elongation factor 1alpha from a low thermophilic Sulfolobus solfataricus strain
FEMS Microbiol. Lett.
218
285-290
2003
Saccharolobus solfataricus, Saccharolobus solfataricus (P35021)
Manually annotated by BRENDA team
Bocchini, V.; Adinolfi, B.S.; Arcari, P.; Arcucci, A.; Dello Russo, A.; De Vendittis, E.; Ianniciello, G.; Masullo, M.; Raimo, G.
Protein engineering on enzymes of the peptide elongation cycle in Sulfolobus solfataricus
Biochimie
80
895-898
1998
Saccharolobus solfataricus (P30925), Saccharolobus solfataricus (P35021), Saccharolobus solfataricus (Q64214)
Manually annotated by BRENDA team