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Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.5.4 LamB signal peptide dose-dependent inhibition of GTPase activity Escherichia coli
3.6.5.4 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

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.6.5.4 Escherichia coli
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
3.6.5.4 Ffh
-
 Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.5.4 7.5
-
 assay at Escherichia coli