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Information on EC 3.2.2.22 - rRNA N-glycosylase and Organism(s) Momordica charantia and UniProt Accession P16094
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3.2.2.22 rRNA N-glycosylaseIUBMB 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.
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- 3.2.2.22
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checkpoint
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immunotherapy
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death-ligand
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nsclc
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non-small
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toxin-producing
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monotherapy
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durable
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first-line
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evasion
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immune-related
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non-small-cell
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recist
The taxonomic range for the selected organisms is: Momordica charantia
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
gelonin
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-
-
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Mirabilis antiviral protein
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-
-
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momorcochin-S
-
-
-
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nigrin b
-
-
-
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ribosomal ribonucleate N-glycosidase
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-
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ricin
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-
-
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RNA N-glycosidase
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-
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rRNA N-glycosidase
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-
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saporins
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
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-
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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
113756-12-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA + H2O
?
-
primarily DNA substrate, polynucleotide:adenosine glycosidase activity
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-
?
naked rRNA + H2O
?
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primarily DNA substrate, polynucleotide:adenosine glycosidase activity
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-
?
polyA + H2O
?
-
primarily DNA substrate, polynucleotide:adenosine glycosidase activity
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-
?
rRNA + H2O
?
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a total of 20 and 40 microg of ribosome inactivating protein on 1 square cm discs of Physeolus vulgaris leaves, monitoring of weight gain (day 4 and 10), survival rate, DNA lesions, and oxidative status as catalase and superoxide dismutase activities and lipidic peroxidation in third instar butterfly larvae of Noctuidae Anticarsia gemmatalis and Spodoptera frugiperda
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-
?
supercoiled double-stranded DNA + H2O
nicked and linear forms of DNA
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-
-
-
?
supercoiled double-stranded DNA + H2O
nicked and linear forms of DNA
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highly purified enzymes depurinate extensively pBR322 circular, supercoiled DNA at neutral pH and exhibit neither DNase nor DNA glycosylase activities, DNA modifications other than depurination may be attributed to contamination with nucleases, gelonin, momordin I, PAP-S, and saporin-S6 do not cleave DNA strands, the only base released is adenine, it may be concluded that polynucleotide:adenosine glycosidase is the enzymatic activity on DNA of these, and possibly all, ribosome-inactivating proteins
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-
?
additional information
?
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alpha-momorcharin has both N-glycosidase activity and DNA-nuclease activity
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-
?
additional information
?
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alpha-momorcharin has both N-glycosidase activity and DNA-nuclease activity
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?
additional information
?
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the enzyme binds specifically to terminal Gal and GalNAc of the target cell surface receptor, preferring Gal
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-
?
additional information
?
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enzyme inhibits the growth of the fungus Sphaerotheca fuliginea in vitro
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-
?
additional information
?
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enzyme inhibits the growth of the fungus Sphaerotheca fuliginea in vitro
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-
?
additional information
?
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depurination of rRNA, N-glycosidase activity, oxidative and genotoxic action on butterfly third instar larvae Anticarsia gemmatalis (soybean caterpillar) and Spodoptera frugiperda (fall armyworm) of the lepidopteran family Noctuidae
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-
?
additional information
?
-
-
ribosome-inactivating proteins, RIPs, are a family of enzymes that depurinate rRNA and inhibit protein biosynthesis
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme binds specifically to terminal Gal and GalNAc of the target cell surface receptor, preferring Gal
-
-
?
additional information
?
-
enzyme inhibits the growth of the fungus Sphaerotheca fuliginea in vitro
-
-
?
additional information
?
-
-
enzyme inhibits the growth of the fungus Sphaerotheca fuliginea in vitro
-
-
?
additional information
?
-
-
depurination of rRNA, N-glycosidase activity, oxidative and genotoxic action on butterfly third instar larvae Anticarsia gemmatalis (soybean caterpillar) and Spodoptera frugiperda (fall armyworm) of the lepidopteran family Noctuidae
-
-
?
additional information
?
-
-
ribosome-inactivating proteins, RIPs, are a family of enzymes that depurinate rRNA and inhibit protein biosynthesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme requires divalent metal ions for activity
additional information
-
the enzyme requires divalent metal ions for activity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
momordin: increase in cells that show DNA damage in both species, reduced weight in Anticarsia gemmatalis at day 10 with 40 microg, in Spodoptera frugiperda superoxide dismutase inhibition to 20% with 40 microg
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
alpha-momorcharin can inhibit the mycelial growth of Fusarium solani, Fusarium oxysporum, and Pseudomonas aeruginosa
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RIP1_MOMCH
286
0
31532
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
construction of enzyme-PEG conjugates and immunogenicity analysis, overview. RIP-PEG conjugates show a strong anti-tumor activity through apoptotic pathway like RIP, buts with less toxicity to normal cells and reduced antigenicity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from seeds by ammonium sulfate fractionation, and two steps of gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
study on conformation of partially unfolded state through steady-state and time-resolved fluorescence spectroscopy on a single Trp-190 which is located adjacently to the active site. The transient folding/unfolding intermediate state of beta-momorcharin adopts a specific conformation at the vicinity of the active site
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Endo, Y.; Tsurugi, K.; Lambert, J.M.
The site of action of six different ribosome-inactivating proteins from plants on eukaryotic ribosomes: the RNA N-glycosidase activity of the proteins
Biochem. Biophys. Res. Commun.
150
1032-1036
1988
Suregada multiflora, Momordica charantia, Phytolacca americana, Saponaria officinalis
Barbieri, L.; Valbonesi, P.; Righi, F.; Zuccheri, G.; Monti, F.; Gorini, P.; Samori, B.; Stirpe, F.
Polynucleotide:Adenosine glycosidase is the sole activity of ribosome-inactivating proteins on DNA
J. Biochem.
128
883-889
2000
Suregada multiflora, Momordica charantia, Phytolacca americana, Saponaria officinalis
Peumans, W.J.; Hao, Q.; Van Damme, E.J.
Ribosome-inactivating proteins from plants: more than RNA N-glycosidases?
FASEB J.
15
1493-1506
2001
Abrus precatorius, Ricinus communis, Eranthis hyemalis, Suregada multiflora, Hordeum vulgare, Momordica charantia, no activity in Arabidopsis thaliana, Phytolacca americana, Phytolacca insularis, Saponaria officinalis, Trichosanthes kirilowii, Trichosanthes sp.
Hartley, M.R.; Lord, J.M.
Cytotoxic ribosome-inactivating lectins from plants
Biochim. Biophys. Acta
1701
1-14
2004
Abrus precatorius, Cucurbita pepo, Dianthus caryophyllus, Escherichia coli, Mirabilis jalapa, Momordica charantia, Phytolacca americana, Sambucus nigra, Saponaria officinalis, Shigella dysenteriae, Trichosanthes kirilowii, Triticum aestivum, Viscum album, Adenia volkensii, Sambucus ebulus, Ricinus communis (P02879)
Xu, J.; Wang, H.; Fan, J.
Expression of a ribosome-inactivating protein gene in bitter melon is induced by Sphaerotheca fuliginea and abiotic stimuli
Biotechnol. Lett.
29
1605-1610
2007
Momordica charantia (P24817), Momordica charantia
Fukunaga, Y.; Nishimoto, E.; Yamashita, K.; Otosu, T.; Yamashita, S.
The partially unfolded state of beta-momorcharin characterized with steady-state and time-resolved fluorescence studies
J. Biochem.
141
9-18
2007
Momordica charantia
Bertholdo-Vargas, L.R.; Martins, J.N.; Bordin, D.; Salvador, M.; Schafer, A.E.; Barros, N.M.; Barbieri, L.; Stirpe, F.; Carlini, C.R.
Type 1 ribosome-inactivating proteins - entomotoxic, oxidative and genotoxic action on Anticarsia gemmatalis (Huebner) and Spodoptera frugiperda (J.E. Smith) (Lepidoptera: Noctuidae)
J. Insect Physiol.
55
51-58
2009
Suregada multiflora, Momordica charantia, Phytolacca americana, Saponaria officinalis, Silene chalcedonica
Li, M.; Chen, Y.; Liu, Z.; Shen, F.; Bian, X.; Meng, Y.
Anti-tumor activity and immunological modification of ribosome-inactivating protein (RIP) from Momordica charantia by covalent attachment of polyethylene glycol
Acta Biochim. Biophys. Sin. (Shanghai)
41
792-799
2009
Momordica charantia
Wang, S.; Zhang, Y.; Liu, H.; He, Y.; Yan, J.; Wu, Z.; Ding, Y.
Molecular cloning and functional analysis of a recombinant ribosome-inactivating protein (alpha-momorcharin) from Momordica charantia
Appl. Microbiol. Biotechnol.
96
939-950
2012
Momordica charantia (P16094), Momordica charantia
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