Literature summary for 3.2.2.22 extracted from

Chambery, A.; Pisante, M.; Di Maro, A.; Di Zazzo, E.; Ruvo, M.; Costantini, S.; Colonna, G.; Parente, A.
Invariant Ser211 is involved in the catalysis of PD-L4, type I RIP from Phytolacca dioica leaves (2007), Proteins, 67, 209-218.

Search for more literature for 3.2.2.22

Crystallization (Commentary)

Crystallization (Comment)	Organism
modeling and docking analysis on interaction of residue S211 with W207 located within the active site	Phytolacca dioica

Protein Variants

Protein Variants	Comment	Organism
S211A	no influence on N-beta-glycosidase activity, but reduction of adenine polynucleotide glycosylase activity. Residual activity on deadenylation is 33% on polyA, 73% on DNA, and 66% on rRNA	Phytolacca dioica

Organism

Organism	UniProt	Comment	Textmining
Phytolacca dioica	P84854	PD-L4, type I ribosome inactivating protein	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Phytolacca dioica	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
28S rRNA + H2O	-	Phytolacca dioica	?	-	?
DNA + H2O	-	Phytolacca dioica	?	-	?
polyA + H2O	-	Phytolacca dioica	?	-	?

Synonyms

Synonyms	Comment	Organism
PD-L4	-	Phytolacca dioica

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)