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Literature DB >> 3902015

Vitamin K (menaquinone) biosynthesis in bacteria: purification and probable structure of an intermediate prior to o-succinylbenzoate.

Abstract

The first aromatic intermediate in the menaquinone biosynthetic pathway is o-succinylbenzoate (OSB); it is formed from chorismate/isochorismate and 2-ketoglutarate. Cell-free extracts of menD+ E. coli strains synthesize an intermediate, "X", which is converted to OSB by extracts of menC+ cells. "X" has been purified to near homogeneity by HPLC. On treatment with acid, it yields both OSB and succinylbenzene (SB). This and other data, suggest that "X" has the structure, 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (I).

Entities: Chemical Gene Species

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Year: 1985 PMID： 3902015 DOI： 10.1016/0006-291x(85)91332-4

Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575

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Cited

8 in total

1. Sequence and overexpression of the menD gene from Escherichia coli.

Authors: J L Popp
Journal: J Bacteriol Date: 1989-08 Impact factor: 3.490

2. Biosynthesis of o-succinylbenzoic acid in Bacillus subtilis: identification of menD mutants and evidence against the involvement of the alpha-ketoglutarate dehydrogenase complex.

Authors: C Palaniappan; H Taber; R Meganathan
Journal: J Bacteriol Date: 1994-05 Impact factor: 3.490

3. Menaquinone (vitamin K2) biosynthesis: cloning, nucleotide sequence, and expression of the menC gene from Escherichia coli.

Authors: V Sharma; R Meganathan; M E Hudspeth
Journal: J Bacteriol Date: 1993-08 Impact factor: 3.490

4. Menaquinone (vitamin K2) biosynthesis: evidence that the Escherichia coli menD gene encodes both 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid synthase and alpha-ketoglutarate decarboxylase activities.

Authors: C Palaniappan; V Sharma; M E Hudspeth; R Meganathan
Journal: J Bacteriol Date: 1992-12 Impact factor: 3.490

5. Crystallization and preliminary X-ray analysis of (1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) synthase (MenD) from Escherichia coli.

Authors: Edyta A L Sieminska; Andrea Macova; David R J Palmer; David A R Sanders
Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Date: 2005-04-22

Vitamin K (menaquinone) biosynthesis in bacteria: purification and probable structure of an intermediate prior to o-succinylbenzoate.

1. Sequence and overexpression of the menD gene from Escherichia coli.

2. Biosynthesis of o-succinylbenzoic acid in Bacillus subtilis: identification of menD mutants and evidence against the involvement of the alpha-ketoglutarate dehydrogenase complex.

3. Menaquinone (vitamin K2) biosynthesis: cloning, nucleotide sequence, and expression of the menC gene from Escherichia coli.

4. Menaquinone (vitamin K2) biosynthesis: evidence that the Escherichia coli menD gene encodes both 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid synthase and alpha-ketoglutarate decarboxylase activities.

5. Crystallization and preliminary X-ray analysis of (1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) synthase (MenD) from Escherichia coli.

6. Biosynthesis of Menaquinone (Vitamin K2) and Ubiquinone (Coenzyme Q).

7. Biosynthesis of Menaquinone in E. coli: Identification of an Elusive Isomer of SEPHCHC.

8. Menaquinone and iron are essential for complex colony development in Bacillus subtilis.