Literature summary for 3.2.2.22 extracted from

Vandenbussche, F.; Desmyter, S.; Ciani, M.; Proost, P.; Peumans, W.J.; Van Damme, E.J.
Analysis of the in planta antiviral activity of elderberry ribosome-inactivating proteins (2004), Eur. J. Biochem., 271, 1508-1515.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of SNA-I, SNA-IV, SNA-V, and SNLRP in Nicotiana tabacum cv. Samsun NN transgenic plants, expression levels, overview	Sambucus nigra

Protein Variants

Protein Variants	Comment	Organism
additional information	generation of Nicotiana tabacum cv. Samsun NN transgenic plants expressing SNA-I, SNA-IV, SNA-V, and SNLRP in leaves, the transgenic plants show anti-viral activity against the tobacco mosaic virus due to the recombinant polynucleotide-adenosine glycosylase activity, overview	Sambucus nigra

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
tobacco mosaic virus RNA + H2O	Sambucus nigra	SNA-I, SNA-V, and SNLRP show anti-viral activity	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Sambucus nigra	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant SNA-I, SNA-IV, SNA-V, and SNLRP from Nicotiana tabacum cv. Samsun NN transgenic plants by ion exchange chromatography, and fetuin affinity chromatography for SNA-I, recombinant SNA-IV and SNA-V are purified by ammonium sulfate fractionation, galactose affinity chromatography, and hydrophobic interaction chromatography, recombinant SNLRP is purified by ion exchange chromatography and gel filtration	Sambucus nigra

Purification (Comment)

Organism

recombinant SNA-I, SNA-IV, SNA-V, and SNLRP from Nicotiana tabacum cv. Samsun NN transgenic plants by ion exchange chromatography, and fetuin affinity chromatography for SNA-I, recombinant SNA-IV and SNA-V are purified by ammonium sulfate fractionation, galactose affinity chromatography, and hydrophobic interaction chromatography, recombinant SNLRP is purified by ion exchange chromatography and gel filtration

Sambucus nigra

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	purified recombinant SNA-I shows very low activity, purified recombinant SNA-IV is inactive, TMV anti-viral activity of recombinant RIPs, overview	Sambucus nigra
0.000011	-	purified recombinant SNA-V, substrate tobacco mosaic virus RNA, polynucleotide-adenosine glycosylase activity	Sambucus nigra
0.000014	-	purified recombinant SNLRP, substrate tobacco mosaic virus RNA, polynucleotide-adenosine glycosylase activity	Sambucus nigra

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
additional information	the elderberry type-2 ribosome-inactivating proteins SNA-I, SNA-V, and SNLRP are devoid of all rRNA N-glycosylase activity towards plant ribosomes, SNLRP possesses no sugar binding activity in contrast to SNA-I and SNA-V	Sambucus nigra	?	-	?
tobacco mosaic virus RNA + H2O	SNA-I, SNA-V, and SNLRP show anti-viral activity	Sambucus nigra	?	-	?
tobacco mosaic virus RNA + H2O	SNA-I, SNA-V, and SNLRP show polynucleotide-adenosine glycosylase activity, i.e. PAG activity, releasing adenine	Sambucus nigra	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 30000-35000, recombinant SNA-I, SNA-IV, SNA-V, and SNLRP, SDS-PAGE	Sambucus nigra

Synonyms

Synonyms	Comment	Organism
SNA-I	-	Sambucus nigra
SNA-V	-	Sambucus nigra
SNLRP	-	Sambucus nigra
type 2 ribosome-inactivating protein	-	Sambucus nigra
type II ribosome-inactivating protein	-	Sambucus nigra
type-2 RIP	-	Sambucus nigra

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	polynucleotide-adenosine glycosylase activity assay at	Sambucus nigra

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
4	-	polynucleotide-adenosine glycosylase activity assay at	Sambucus nigra