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Literature summary for 3.4.21.B50 extracted from

  • Sun, R.; Fan, H.; Gao, F.; Lin, Y.; Zhang, L.; Gong, W.; Liu, L.
    Crystal structure of Arabidopsis Deg2 protein reveals an internal PDZ ligand locking the hexameric resting state (2012), J. Biol. Chem., 287, 37564-37569.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.B50

Cloned(Commentary)

Cloned (Comment) Organism
gene deg2, recombinant expression of the maltose-binding protein- and His6-tagged enzyme in Escherichia coli Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast stroma
-
 Arabidopsis thaliana 9570
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana O92261 gene deg2
-

Purification (Commentary)

Purification (Comment) Organism
recombinant maltose-binding protein- and His6-tagged enzyme from Escherichia coli by dextrin affinity chromatography, folloed by tag cleavage through tobacco etch virus protease Arabidopsis thaliana

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-casein + H2O the enzyme is able to specifically degrade beta-casein but not alpha-casein Arabidopsis thaliana ?
-
 ?
additional information the enzyme shows chaperone-like activity, its presence reduces the aggregation of the DTT-denatured lysozyme Arabidopsis thaliana ?
-
 ?

Subunits

Subunits Comment Organism
hexamer or dodecamer hexameric structure of mature enzyme, the Deg2 hexamer exists predominantly during substrate incubation in a resting state,the large oligomeric state is the active state, model of oligomeric state change, overview Arabidopsis thaliana
More structure-function analysis of the dimerization interface between Deg2 trimers, overview. The enzyme contains a unique second PDZ domain (PDZ2) following a conventional PDZ domain (PDZ1), with PDZ2 orchestrating the cage assembly of the enzyme, a conserved internal ligand for PDZ2 mediates hexamer formation and locks the protease in the resting state. Because loop JK lies outside the hexamer shell, it provides protection for the loop LA-PDZ2 interface from solvents and may play a role in changes in the oligomeric enzyme state Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
DEG2
-
 Arabidopsis thaliana
Deg2 protease
-
 Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Arabidopsis thaliana

pH Range

pH Minimum pH Maximum Comment Organism
6 9.5 activity range Arabidopsis thaliana

General Information

General Information Comment Organism
additional information The Deg2 protease domain consists of a catalytic triad comprising His159, Asp190, and Ser268. The enzyme contains a unique second PDZ domain (PDZ2) following a conventional PDZ domain (PDZ1), with PDZ2 orchestrating the cage assembly of the enzyme, a conserved internal ligand for PDZ2 mediates hexamer formation and locks the protease in the resting state Arabidopsis thaliana
physiological function the enzyme's proteolytic activity in the chloroplast stroma is required to maintain the efficiency of photosynthetic machinery during stress, the enzyme exhibits dual protease-chaperone activities Arabidopsis thaliana