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Literature summary for 3.4.22.34 extracted from

  • Zauner, F.B.; Dall, E.; Regl, C.; Grassi, L.; Huber, C.G.; Cabrele, C.; Brandstetter, H.
    Crystal structure of plant legumain reveals a unique two-chain state with pH-dependent activity regulation (2018), Plant Cell, 30, 686-699 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.34

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression in a fully N-glycosylated form Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapor-diffusion method Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
vacuole
-
 Arabidopsis thaliana 5773
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q39119
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification mechanisms of autoactivation, including a plant-specific two-chain activation state, which remains conformationally stable at neutral pH, which is a prerequisite for full ligase activity and survival in different cell compartments Arabidopsis thaliana

Purification (Commentary)

Purification (Comment) Organism
-
 Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme has protease activity and efficient peptide bond ligase activity Arabidopsis thaliana ?
-
 ?

Synonyms

Synonyms Comment Organism
AtLEGgamma
-
 Arabidopsis thaliana

General Information

General Information Comment Organism
physiological function important roles in many physiological processes, including programmed cell death Arabidopsis thaliana