Biochemical study on ubiquinone biosynthesis in Escherichia coli: I. Specificity of para hydroxybenzoate polyprenyltransferase

Hachimi, Zakia El; Samuel, O.; Azerad, Robert

doi:10.1016/s0300-9084(74)80017-9

Cited by 18 publications

(11 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The enzyme responsible for this conversion was named 3-octaprenyl-4-hydroxybenzoate decarboxylase. The presence of decarboxylase was also observed by El Hachimi et al (35). The enzyme activity was absent in ubiD mutants (26).…”

Section: Formation Of 2-octaprenylphenol (Compound XXI -------->Xxii)supporting

confidence: 66%

“…The enzyme is membrane bound and requires octaprenyl diphosphate and Mg 2+ (175). In addition to octaprenyl diphosphate, the enzyme could incorporate geranyl, farnesyl, phytyl, or solanesyl diphosphate as a side chain precursor (35,111). This lack of specificity also extends to the aromatic substrate; thus, 4-aminobenzoate can replace 4-hydroxybenzoate as a substrate (35).…”

Section: Prenylation Of 4-hydroxybenzoate (Compound Xx-------->xxi)mentioning

confidence: 99%

See 1 more Smart Citation

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

Meganathan¹,

Kwon²

2009

EcoSal

View full text Add to dashboard Cite

Section: Formation Of 2-octaprenylphenol (Compound XXI -------->Xxii)supporting

confidence: 66%

Section: Prenylation Of 4-hydroxybenzoate (Compound Xx-------->xxi)mentioning

confidence: 99%

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

Meganathan¹,

Kwon²

2009

EcoSal

View full text Add to dashboard Cite

“…An ubiA mutant of E. coli was found to accumulate DMK but not MK. This mutant is believed to be defective in methylation of DMK to MK, suggesting that this is a double mutant (35). In a subsequent study, it was shown that an ubiE mutant, blocked in the methylation of the ubiquinone biosynthetic intermediate, 2-octaprenyl-6-methoxy-1,4-benzoquinol (OMB) (XXV) to 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol (OMMB) (XXVI) (174) accumulated DMK but not MK (171).…”

Section: Mk Biosynthesismentioning

confidence: 99%

“…In addition to octaprenyl diphosphate, the enzyme could incorporate geranyl, farnesyl, phytyl, or solanesyl diphosphate as a side chain precursor (35, 111). This lack of specificity also extends to the aromatic substrate; thus, 4-aminobenzoate can replace 4-hydroxybenzoate as a substrate (35). Recently, it has been shown that the enzyme accepts a wide variety of benzoic acid derivatives as substrates.…”

Section: Q Biosynthesismentioning

confidence: 99%

See 1 more Smart Citation

Biosynthesis of Menaquinone (Vitamin K ₂ ) and Ubiquinone (Coenzyme Q)

Meganathan

Kwon

2009

EcoSal Plus

View full text Add to dashboard Cite

Escherichia coli and Salmonella contain the naphthoquinones menaquinone (MK; vitamin K 2 ) and demethylmenaquinone and the benzoquinone ubiquinone (coenzyme Q; Q). Both quinones are derived from the shikimate pathway, which has been called a "metabolic tree with many branches." There are two different pathways for the biosynthesis of the naphthoquinones. The vast majority of prokaryotes, including E. coli and Salmonella , and the plants use the o -succinylbenzoate pathway, while a minority uses the futalosine pathway. The quinone nucleus of Q is derived directly from chorismate, while that of MK is derived from chorismate via isochorismate. The prenyl side chains of both quinones are from isopentenyl diphosphate formed by the 2- C -methyl-D-erythritol 4-phosphate (non-mevalonate) pathway and the methyl groups are from S -adenosylmethionine. In addition, MK biosynthesis requires 2-ketoglutarate and cofactors ATP, coenzyme A, and thiamine pyrophosphate. Despite the fact that both quinones originate from the shikimate pathway, there are important differences in their biosyntheses. The prenyl side chain in MK biosynthesis is introduced at the penultimate step, accompanied by decarboxylation, whereas in Q biosynthesis it is introduced at the second step, with retention of the carboxyl group. In MK biosynthesis, all the reactions of the pathway up to prenylation are carried out by soluble enzymes, whereas all the enzymes involved in Q biosynthesis except the first are membrane bound. In MK biosynthesis, the last step is a C -methylation; in Q biosynthesis, the last step is an O -methylation. In Q biosynthesis a second C -methylation and O -methylation take place in the middle part of the pathway. Despite the fact that Q and MK biosyntheses diverge at chorismate, the C -methylations in both pathways are carried out by the same methyltransferase.

show abstract