Literature summary for 1.3.98.1 extracted from

Ottosen, M.B.; Bjornberg, O.; Norager, S.; Larsen, S.; Palfey, B.A.; Jensen, K.F.
The dimeric dihydroorotate dehydrogenase A from Lactococcus lactis dissociates reversibly into inactive monomers (2002), Protein Sci., 11, 2575-2583.

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Protein Variants

Protein Variants	Comment	Organism
E206/K296E	conversion of intermolecular salt bridge, mutant is fully active in concentrated solutions and dissociates into monomers upon dilution like wild-type enzyme	Lactococcus lactis
E206A	disturbance of intermolecular salt bridge, mutant retains almost complete activity	Lactococcus lactis
E206K	disturbance of intermolecular salt bridge, mutant activity is severely impaired	Lactococcus lactis
K296A	disturbance of intermolecular salt bridge, mutant retains almost complete activity	Lactococcus lactis
K296E	disturbance of intermolecular salt bridge, mutant activity is severely impaired	Lactococcus lactis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
67000	-	gel filtration	Lactococcus lactis

Organism

Organism	UniProt	Comment	Textmining
Lactococcus lactis	-	-	-

Subunits

Subunits	Comment	Organism
More	in concentrated solutions, dimer, reversible dissociation into inactive monomers upon dilution, orotate protects	Lactococcus lactis

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Release 2023.1 (January 2023)