Literature summary for 4.4.1.5 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.

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Activating Compound

Activating Compound	Comment	Organism	Structure
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

Application	Comment	Organism
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

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

Metals/Ions

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

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	-	-	-

Subunits

Subunits	Comment	Organism
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
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

Synonyms	Comment	Organism
glyoxalase I	-	Pseudomonas putida

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Release 2023.1 (January 2023)