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Literature summary for 3.6.5.4 extracted from

  • Swain, J.F.; Gierasch, L.M.
    Signal peptides bind and aggregate RNA. An alternative explanation for GTPase inhibition in the signal recognition particle (2001), J. Biol. Chem., 276, 12222-12227.
    View publication on PubMed
Search for more literature for 3.6.5.4

Inhibitors

Inhibitors Comment Organism Structure
LamB signal peptide dose-dependent inhibition of GTPase activity Escherichia coli
signal peptide isolated functional signal peptides bind nonspecifically to the RNA component of SRP and aggregate the entire signal recognition particle, leading to a loss of its intrinsic GTPase activity, this effect is an artifact of the high peptide concentrations and low salt conditions used in in vitro studies, signal sequences at the N-terminus of nascent chains in vivo do not exhibit this activity Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Escherichia coli protein targeting to the plasma membrane GDP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
 Escherichia coli GDP + phosphate
-
 ?
GTP + H2O protein targeting to the plasma membrane Escherichia coli GDP + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
Ffh
-
 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli