IPR004433
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase
InterPro entry
Short name | MenaQ_synth_MenD |
Description
MenD was thought to act as SHCHC synthase, but has recently been shown 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. 2-oxoglutarate decarboxylase/SHCHC synthase (menD) is a thiamine pyrophosphate enzyme involved in menaquinone biosynthesis
[1].
References
1.Menaquinone biosynthesis in Escherichia coli: identification of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate as a novel intermediate and re-evaluation of MenD activity. Jiang M, Cao Y, Guo ZF, Chen M, Chen X, Guo Z. Biochemistry 46, 10979-89, (2007). View articlePMID: 17760421
GO terms
biological process
molecular function
cellular component
- None
Cross References
ENZYME
Genome Properties
Contributing Member Database Entries
- PIRSF:PIRSF004983
- HAMAP:MF_01659
- NCBIfam:TIGR00173
Representative structure
5ej8: EcMenD-ThDP-Mn2+ complex structure soaked with 2-ketoglutarate for 2 min