Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.2.22 - rRNA N-glycosylase and Organism(s) Phytolacca dioica and UniProt Accession P84854

for references in articles please use BRENDA:EC3.2.2.22
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.22 rRNA N-glycosylase
IUBMB Comments
Ricin A-chain and related toxins show this activity. Naked rRNA is attacked more slowly than rRNA in intact ribosomes. Naked rRNA from Escherichia coli is cleaved at a corresponding position.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Phytolacca dioica
UNIPROT: P84854
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Phytolacca dioica
The enzyme appears in selected viruses and cellular organisms
Synonyms
pd-l1, ricin, shiga toxin, saporin, abrin, ricinus communis agglutinin, gelonin, ricin a chain, trichosanthin, ribosome-inactivating proteins, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ribosome inactivating protein
-
gelonin
-
-
-
-
Mirabilis antiviral protein
-
-
-
-
momorcochin-S
-
-
-
-
nigrin b
-
-
-
-
PD-L1
ribosomal ribonucleate N-glycosidase
-
-
-
-
ribosome inactivating protein
-
ricin
-
-
-
-
RNA N-glycosidase
-
-
-
-
rRNA N-glycosidase
-
-
-
-
saporins
-
-
-
-
type 1 ribosome-inactivating protein
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
rRNA N-glycohydrolase
Ricin A-chain and related toxins show this activity. Naked rRNA is attacked more slowly than rRNA in intact ribosomes. Naked rRNA from Escherichia coli is cleaved at a corresponding position.
CAS REGISTRY NUMBER
COMMENTARY hide
113756-12-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
28S rRNA + H2O
?
show the reaction diagram
-
-
-
?
DNA + H2O
?
show the reaction diagram
-
-
-
?
hsDNA + H2O
?
show the reaction diagram
-
-
-
?
poly(A) substrate + H2O
?
show the reaction diagram
-
-
-
?
polyA + H2O
?
show the reaction diagram
-
-
-
?
rRNA + H2O
?
show the reaction diagram
Escherichia coli 16S and 23S rRNA
-
-
?
hsDNA + H2O
?
show the reaction diagram
-
-
-
?
poly(A) substrate + H2O
?
show the reaction diagram
-
-
-
?
rRNA + H2O
?
show the reaction diagram
Escherichia coli 16S and 23S rRNA
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RIPL2_PHYDI
261
0
29190
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30360
PD-L 3 measured with ESI-Q-TOF MS, including two disulfide bridges (-4) and two glycosidic chains (+2342), corresponding to calculated value of amino acids 29190 Da
31560
PD-L 2 measured with ESI-Q-TOF MS, including two disulfide bridges (-4) and two glycosidic chains (+2342), corresponding to calculated value of amino acids 29222 Da
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling and docking analysis on interaction of residue S211 with W207 located within the active site
space group C2, two molecules per asymmetric unit
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from spring leaf
-
recombinant isozymes from Escherichia coli strain BL21(DE3), purification after overexpression affords refolding by glutathione in refolding buffer, followd by ultrafiltration and cation exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of isozymes in Escherichia coli strain BL21(DE3). Synthesis and expression of a PD-L1 synthetic gene in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ruggieroa, A.; Chambery, A.; Di Maro, A.; Mastroianni, A.; Parente, A.; Berisio, R.
Crystallization and preliminary X-ray diffraction analysis of PD-L1, a highly glycosylated ribosome inactivating protein with DNase activity
Protein Pept. Lett.
14
407-409
2007
Phytolacca dioica
Manually annotated by BRENDA team
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
Proteins
67
209-218
2007
Phytolacca dioica (P84854), Phytolacca dioica
Manually annotated by BRENDA team
Di Maro, A.; Chambery, A.; Carafa, V.; Costantini, S.; Colonna, G.; Parente, A.
Structural characterization and comparative modeling of PD-Ls 1-3, type 1 ribosome-inactivating proteins from summer leaves of Phytolacca dioica L
Biochimie
91
352-363
2009
Phytolacca dioica (P84853), Phytolacca dioica (P84854), Phytolacca dioica
Manually annotated by BRENDA team
Severino, V.; Chambery, A.; Di Maro, A.; Marasco, D.; Ruggiero, A.; Berisio, R.; Giansanti, F.; Ippoliti, R.; Parente, A.
The role of the glycan moiety on the structure-function relationships of PD-L1, type 1 ribosome-inactivating protein from P. dioica leaves
Mol. Biosyst.
6
570-579
2010
Phytolacca dioica (P84853), Phytolacca dioica
Manually annotated by BRENDA team