Literature summary for 2.6.1.52 extracted from

Mishra, V.; Kumar, A.; Ali, V.; Nozaki, T.; Zhang, K.Y.; Bhakuni, V.
Novel protein-protein interactions between Entamoeba histolyticad-phosphoglycerate dehydrogenase and phosphoserine aminotransferase (2012), Biochimie, 94, 1676-1686.

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Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
155000	-	gel filtration, protein-protein complex with D-phosphoglycerate dehydrogenase, which has a 1:1 stoichiometry	Entamoeba histolytica

Organism

Organism	UniProt	Comment	Textmining
Entamoeba histolytica	-	-	-

Subunits

Subunits	Comment	Organism
More	enzyme forms a protein-protein complex with D-phosphoglycerate dehydrogenase, which has a 1:1 stoichiometry. Ionic interactions play a significant role in complex formation and stability. The nucleotide binding domain of D-phosphoglycerate dehydrogenase specifically interacts with the enzyme. The purified nucleotide binding domain of D-phosphoglycerate dehydrogenase interacts with phosphoserine transaminase. The reactions catalyzed by the complex suggest a possibility of substrate channelling in the protein complex	Entamoeba histolytica

General Information

General Information	Comment	Organism
physiological function	enzyme forms a protein-protein complex with D-phosphoglycerate dehydrogenase, which has a 1:1 stoichiometry. Ionic interactions play a significant role in complex formation and stability. The nucleotide binding domain of D-phosphoglycerate dehydrogenase specifically interacts with the enzyme. The purified nucleotide binding domain of D-phosphoglycerate dehydrogenase interacts with phosphoserine transaminase. The reactions catalyzed by the complex suggest a possibility of substrate channelling in the protein complex	Entamoeba histolytica

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Release 2023.1 (January 2023)