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Literature summary extracted from

  • Yang, Y.; Mak, A.N.; Shaw, P.C.; Sze, K.H.
    Solution structure of an active mutant of maize ribosome-inactivating protein (MOD) and its interaction with the ribosomal stalk protein P2 (2010), J. Mol. Biol., 395, 897-907.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.2.22 additional information maize RIP, a type III RIP, is unique compared to the other type I and type II RIPs, because it is synthesized as a precursor with a 25-residue internal inactivation region, which is removed in order to activate the protein Zea mays

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.2.22 additional information maize RIP, a type III RIP, is unique compared to the other type I and type II RIPs, because it is synthesized as a precursor with a 25-residue internal inactivation region, which is removed in order to activate the protein Zea mays

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.2.22 additional information Zea mays ribosome-inactivating proteins, RIPs, are N-glycosidases that depurinate a specific adenine residue in the conserved sarcin/ricin loop of ribosomal RNA ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.22 Zea mays
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.2.22 proteolytic modification maize RIP, a type III RIP, is unique compared to the other type I and type II RIPs, because it is synthesized as a precursor with a 25-residue internal inactivation region, which is removed in order to activate the protein Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.22 additional information ribosome-inactivating proteins, RIPs, are N-glycosidases that depurinate a specific adenine residue in the conserved sarcin/ricin loop of ribosomal RNA Zea mays ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.2.22 More MOD structure determination and comparison using the crystal structure of DELTAN5-MOD, PDB ID 2PQI, and by determination of the NMR solution structure of MOD, PDB ID 2k6H, detailed overview. MOD has shorter beta6 and alphaB segments, probably for accommodating easier substrate binding, and an alpha-helix instead of an antiparallel beta-sheet in the C-terminal domain, which is involved in binding ribosomal protein P2 in some RIPs, compared to type I and II RIPs. The P2 binding site on MOD is located at the N-terminal domain near the internal inactivation region Zea mays

Synonyms

EC Number Synonyms Comment Organism
3.2.2.22 MOD
-
 Zea mays
3.2.2.22 ribosome inactivating protein
-
 Zea mays
3.2.2.22 RIP
-
 Zea mays
3.2.2.22 type III RIP
-
 Zea mays