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Middle domain of thiamine pyrophosphate
TPP_enzyme_M_2 is the middle domain of thiamine pyrophosphate in sequences not captured by Pfam:PF00205. This enzyme is necessary for the first step of the biosynthesis of menaquinone, or vitamin K2, an important cofactor in electron transport in bacteria [1]. [1]. 18983854. Specificity and reactivity in menaquinone biosynthesis: the structure of Escherichia coli MenD (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxyla te synthase). Dawson A, Fyfe PK, Hunter WN;. J Mol Biol. 2008;384:1353-1368. (from Pfam)
thiamine pyrophosphate-dependent enzyme
thiamine pyrophosphate-binding protein
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase catalyzes the thiamin diphosphate (TPP)-dependent decarboxylative carboligation of alpha-ketoglutarate and isochorismate in the menaquinone biosynthetic pathway
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase
MenD was once thought to act as SHCHC synthase, but was shown in 2007 to act instead as SEPHCHC synthase. Conversion of SEPHCHC into SHCHC and pyruvate may occur spontaneously but is catalyzed efficiently, at least in some organisms, by MenH (see TIGR03695).
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