Literature summary for 3.2.2.22 extracted from

Dai, J.; Zhao, L.; Yang, H.; Guo, H.; Fan, K.; Wang, H.; Qian, W.; Zhang, D.; Li, B.; Wang, H.; Guo, Y.
Identification of a novel functional domain of ricin responsible for its potent toxicity (2011), J. Biol. Chem., 286, 12166-12171.

Search for more literature for 3.2.2.22

Application

Application	Comment	Organism
medicine	the conserved alpha-helix is considered as a potential target for the prevention and treatment of ribosome-inactivating protein poisoning	Ricinus communis

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Ricinus communis

Organism

Organism	UniProt	Comment	Textmining
Ricinus communis	P02879	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Ricinus communis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the flexibility of the alpha-helix is responsible for controlling the depurination activity of ricin and determining the extent of protein synthesis inhibition	Ricinus communis	?	-	?
rRNA + H2O	-	Ricinus communis	?	-	?

Synonyms

Synonyms	Comment	Organism
depurinating rRNA N-glycosidase	-	Ricinus communis
ribosome-inactivating protein	-	Ricinus communis
ricin	-	Ricinus communis
RIP	-	Ricinus communis
RTA	ricin A chain	Ricinus communis

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Release 2023.1 (January 2023)