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Literature summary for 3.6.5.3 extracted from

  • Hunter, S.E.; Spremulli, L.L.
    Effects of mutagenesis of residue 221 on the properties of bacterial and mitochondrial elongation factor EF-Tu (2004), Biochim. Biophys. Acta, 1699, 173-182.
    View publication on PubMed
Search for more literature for 3.6.5.3

Cloned(Commentary)

Cloned (Comment) Organism
high level expression of mutant enzyme P269S in Escherichia coli Bos taurus

Protein Variants

Protein Variants Comment Organism
P269S variant is expressed to a high level in Escherichia coli. The variant functions as effectively as the respective wild-type factor in ternary complex formation using Escherichia coli Phe-tRNAPhe and Cys-tRNACys. The variant is also active in A-site binding and in vitro translation assay with Escherichia coli Phe-tRNAPhe Bos taurus
S221P variant is poorly expressed and the majority of molecules fail to fold into an active conformation. The variant functions as effectively as the respective wild-type factor in ternary complex formation using Escherichia coli Phe-tRNAPhe and Cys-tRNACys. The variant is also active in A-site binding and in vitro translation assay with Escherichia coli Phe-tRNAPhe Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Bos taurus 5739
-

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Escherichia coli
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Bos taurus
-

Synonyms

Synonyms Comment Organism
EF-Tu
-
 Escherichia coli
EF-Tumt
-
 Bos taurus