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Literature summary for 2.2.1.9 extracted from

  • Priyadarshi, A.; Saleem, Y.; Nam, K.H.; Kim, K.S.; Park, S.Y.; Kim, E.E.; Hwang, K.Y.
    Structural insights of the MenD from Escherichia coli reveal ThDP affinity (2009), Biochem. Biophys. Res. Commun., 380, 797-801.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli BL21 Escherichia coli K-12

Crystallization (Commentary)

Crystallization (Comment) Organism
tetragonal crystal form Escherichia coli K-12

General Stability

General Stability Organism
2-oxoglutarate improves protein stability Escherichia coli K-12
FAD improves protein stability Escherichia coli K-12
thiamine diphosphate improves protein stability Escherichia coli K-12

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
62000
-
SDS-PAGE Escherichia coli K-12

Organism

Organism UniProt Comment Textmining
Escherichia coli K-12 P17109
-
-

Purification (Commentary)

Purification (Comment) Organism
first step His-Trap chromatography, second step ion-exchange chromatography with Q column, third step chromatography with Superdex column Escherichia coli K-12

Subunits

Subunits Comment Organism
? dimer or tetramer Escherichia coli K-12

Synonyms

Synonyms Comment Organism
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase
-
Escherichia coli K-12
MenD
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Escherichia coli K-12

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
melting temperature 53°C, melting temperature 57.3°C of protein complex with thiamin diphosphate, melting temperature 54°C of protein complex with 2-oxoglutarate, melting temperature 54.5°C of protein complex with FAD Escherichia coli K-12