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Literature summary extracted from

  • Saint-Jean, A.P.; Phillips, K.R.; Creighton, D.J.; Stone, M.J.
    Active monomeric and dimeric forms of Pseudomonas putida glyoxalase I: evidence for 3D domain swapping. (1998), Biochemistry, 37, 10345-10353.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.4.1.5 additional information treatment of the dimer with glutathione yields an active monomer. The monomer is metastable and slowly reverts to the active dimer in the absence of glutathione Pseudomonas putida

Application

EC Number Application Comment Organism
4.4.1.5 additional information is able to exist in two alternative domain-swapped forms. Active site and an essential metal binding site are disassembled and reassembled by the process of domain swapping. 3D domain swapping can be regulated by a small organic ligand Pseudomonas putida

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.4.1.5 additional information monomer is metastable and slowly reverts to the active dimer in the absence of glutathione Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.4.1.5 Zn2+ two zinc ions per dimer. The zinc is required for structure and function. The monomer contains a single zinc ion Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
4.4.1.5 Pseudomonas putida
-
-
-

Subunits

EC Number Subunits Comment Organism
4.4.1.5 dimer treatment of the dimer with glutathione yields an active monomer. The monomer is metastable and slowly reverts to the active dimer in the absence of glutathione Pseudomonas putida
4.4.1.5 monomer treatment of the dimer with glutathione yields an active monomer. The monomer is metastable and slowly reverts to the active dimer in the absence of glutathione Pseudomonas putida

Synonyms

EC Number Synonyms Comment Organism
4.4.1.5 glyoxalase I
-
 Pseudomonas putida