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Literature summary for 2.2.1.9 extracted from

  • Sieminska, E.A.; Macova, A.; Palmer, D.R.; Sanders, D.A.
    Crystallization and preliminary X-ray analysis of (1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) synthase (MenD) from Escherichia coli (2005), Acta Crystallogr. Sect. F, 61, 489-492.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization of the apoenzyme and holoenzyme forms of MenD. The apoenzyme crystals are obtained by sitting-drop vapour diffusion with 70% MPD. The crystals are too small to collect diffraction data and a search for better conditions is not successful. Single crystals of the holoenzyme with thiamin diphosphate and Mn2+ as cofactors are obtained by the hanging-drop vapour-diffusion method with 35% ethylene glycol as precipitant. Diffraction data are collected on a cryocooled crystal to a resolution of 2.0 A Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli MenD participates in the menaquinone (vitamin K2) biosynthetic pathway ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information MenD participates in the menaquinone (vitamin K2) biosynthetic pathway Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
MenD
-
Escherichia coli