Literature summary for 4.6.1.23 extracted from

Miller, S.P.; Bodley, J.W.
Alpha-sarcin cleavage of ribosomal RNA is inhibited by the binding of elongation factor G or thiostrepton to the ribosome (1991), Nucleic Acids Res., 19, 1657-1660 .

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Inhibitors

Inhibitors	Comment	Organism	Structure
elongation factor G	the transitory binding of elongation factor G and GDP to the ribosome inhibits the rate of alpha-sarcin cleavage. The stabilization of this binding with fusidic acid completely prevents alpha-sarcin cleavage	Aspergillus giganteus
GDP	the transitory binding of elongation factor G and GDP to the ribosome inhibits the rate of alpha-sarcin cleavage. The stabilization of this binding with fusidic acid completely prevents alpha-sarcin cleavage	Aspergillus giganteus
Thiostrepton	irreversible binding of the antibiotic thiostrepton to the Escherichia coll ribosome decreases the rate of cleavage by alpha-sarcin approximately 2fold	Aspergillus giganteus

Organism

Organism	UniProt	Comment	Textmining
Aspergillus giganteus	P00655	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Escherichia coli 28S rRNA containing guanosine-adenosine pair + H2O	-	Aspergillus giganteus	an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]	-	?

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Release 2023.1 (January 2023)