Different biosynthetic pathways of the pyrimidine moiety of thiamin in procaryotes and eucaryotes

Yamaada, Kazuko; Morisaki, Mayumi; Kumaoka, Hiroshi

doi:10.1016/0304-4165(83)90022-3

Cited by 23 publications

(13 citation statements)

References 7 publications

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“…In P. putida, E. aerogenes and E. coil, the label of [15N] L -glutamate was incorporated into pyridoxine but not in S, aureus or B, subtilis. The biosynthetic pathway of the pyrimidine moiety of thiamin differs between eukary otes and prokaryotes (10), and the biosynthetic path way of thiazole moiety in eukaryotes and aerobic bacte ria differs from that of facultative anaerobic bacteria (12).…”

Section: Resultsmentioning

confidence: 99%

Biosynthesis of Pyridoxine. Origin of the Nitrogen Atom of Pyridoxine in Microorganisms.

Tanaka

Tazuya

Yamada

et al. 2000

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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SummaryThe amide nitrogen atom of glutamine was incorporated into pyridoxine in four eukaryotes, Emericella nidulans, Mucor racemosus, Neurospora crassa and Saccharomyces cerevisiae, and two prokaryotes, Staphylococcus aureus and Bacillus subtilis, but not in the fol lowing prokaryotes, Pseudomonas putida, Enterobacter aerogenes and Escherichia coll. On the other hand, the nitrogen atom of glutamate was incorporated into pyridoxine in P putida, E.aerogenes and E, coil, but not in S. aureus and B. subtilis. These results suggest that there are at least two different biosynthetic routes for pyridoxine and the difference does not depend on prokaryotes and eukaryotes.

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Section: Resultsmentioning

confidence: 99%

Biosynthesis of Pyridoxine. Origin of the Nitrogen Atom of Pyridoxine in Microorganisms.

Tanaka

Tazuya

Yamada

et al. 2000

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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“…These phosphorylated precursors can be formed in vivo from the corresponding alcohols THZ and HMP. Labeling studies have demonstrated that THZ is derived from glycine (23) and HMP is derived from formate (27). This suggests that THZ biosynthesis is similar to that in yeast and HMP biosynthesis is similar to that in E. coli.…”

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confidence: 98%

Characterization of the Bacillus subtilis thiC operon involved in thiamine biosynthesis

et al. 1997

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The characterization of a three-gene operon (the thiC operon) at 331 min, which is involved in thiamine biosynthesis in Bacillus subtilis, is described. The first gene in the operon is homologous to transcription activators in the lysR family. The second and third genes (thiK and thiC) have been subcloned and overexpressed in Escherichia coli. ThiK (30 kDa) catalyzes the phosphorylation of 4-methyl-5-(␤-hydroxyethyl)thiazole. ThiC (27 kDa) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5-hydroxymethylpyrimidine pyrophosphate by 4-methyl-5-(␤-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. Transcription of the thiC operon is not regulated by thiamine or 2-methyl-4-amino-5-hydroxymethylpyrimidine and is only slightly repressed by 4-methyl-5-(␤-hydroxyethyl)thiazole.Thiamine (THI) pyrophosphate (vitamin B 1 ) is the cofactor required for transketolase, ␣-keto acid decarboxylase, and ␣-keto acid oxidase, enzymes that are important in carbohydrate metabolism (8). In contrast to the situation in Escherichia coli, Salmonella typhimurium, and Saccharomyces species, little is known about the THI biosynthetic pathway in Bacillus subtilis (5). The cofactor is assumed to be formed by linking thiazole (THZ) phosphate (THZ-P) and pyrimidine (HMP) pyrophosphate (HMP-PP) (5) (Fig. 1). These phosphorylated precursors can be formed in vivo from the corresponding alcohols THZ and HMP. Labeling studies have demonstrated that THZ is derived from glycine (23) and HMP is derived from formate (27). This suggests that THZ biosynthesis is similar to that in yeast and HMP biosynthesis is similar to that in E. coli. This is tentative, however, until the origin of all the other atoms of THI has been determined.Three genetic loci involved in the biosynthesis of THI in B. subtilis have been identified: thiA (70 min), thiB (105 min), and thiC (331 min) (11,17,25,29). In feeding experiments, a thiA mutant is HMP requiring, a thiB mutant is THZ requiring, and a thiC mutant is THI requiring. An HMP biosynthetic gene (thiA) has recently been cloned and sequenced and shows high sequence similarity to the E. coli thiC gene (30). None of the other THI biosynthetic genes have been characterized, and the regulation of the pathway has not been studied. As part of the B. subtilis genome sequencing project, a cluster of three genes in the min 331 region of the genome has been cloned and identified as being involved in THI biosynthesis by complementation studies (7). In this paper, we use this sequence information to further characterize this putative three-gene operon. MATERIALS AND METHODSBacterial strains, growth media, and chemicals. B. subtilis wild-type strain CU1065 was a gift from S. Zahler. Minimal growth medium for B. subtilis (CMP) was Spizizen's minimal medium (22)

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“…After each tracer had been added to the medium, the labelled atoms of amino acids in cell protein were calculated. The incorporation rate of the label of [2][3][4][5][6][7][8][9][10][11][12][13] C]-glycine was 37.0% into the thiazole, 33.0% into glycine in protein, and 1.27% into tyrosine in protein. The incorporation rates of thiazole and glycine in protein were therefore very similar.…”

Section: Resultsmentioning

confidence: 99%

“…1) (1)(2)(3)(4)(5). We have previously reported that the biosynthetic pathways of the pyrimidine differ between eukaryotes and prokaryotes (6). In prokaryotes, the pyrimidine is synthesized from 5-aminoimidazole ribonucleotide (AIR), an intermediate of purine biosynthesis (7)(8)(9).…”

mentioning

confidence: 99%

The Biosynthesis of the Thiazole Moiety of Thiamin in the Archaeon <i>Halobacterium salinarum</i>

Hayashi

Kijima

Tazuya-Murayama

et al. 2015

J Nutr Sci Vitaminol

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SummaryThe biosynthetic pathways of the thiazole moiety of thiamin were studied in the archaeon Halobacterium salinarum. Thiamin is generated by the union of 4-amino-5-hydroxymethyl-2-methylpyrimidine (pyrimidine) and 5-(2-hydroxyethyl)-4-methylthiazole (thiazole). The biosynthesis of thiazole is different in facultative anaerobes, aerobes and eukaryotes. In eukaryotes, the C-4, -4′, -5, -5′ and -5″ of the thiazole is biosynthesized from nicotinamide adenine dinucleotide (NAD), with cysteine as S donor and the C-2 and N atoms of glycine. In facultative anaerobic bacteria, such as Escherichia coli, the precursors of the thiazole are the N and C-2 atoms from tyrosine and C-4, -4′, -5, -5′ and -5″ from 1-deoxy-dxylurose-5-phosphate, again with cysteine as S donor. In aerobic bacteria, such as Bacillus subtilis, l-tyrosine is replaced by glycine. In Archaea, known as the third domain of life, the biosynthetic pathway of thiamin has not yet been elucidated. In the present study in the archaeon H. salinarum, it was shown that both the N and C-2 from glycine are incorporated into the thiazole, rather than the N atom coming from l-tyrosine. These results show that thiazole biosynthesis in H. salinarum more closely resembles the biosynthetic pathway found in eukaryotes.

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Different biosynthetic pathways of the pyrimidine moiety of thiamin in procaryotes and eucaryotes

Cited by 23 publications

References 7 publications

Biosynthesis of Pyridoxine. Origin of the Nitrogen Atom of Pyridoxine in Microorganisms.

Biosynthesis of Pyridoxine. Origin of the Nitrogen Atom of Pyridoxine in Microorganisms.

Characterization of the Bacillus subtilis thiC operon involved in thiamine biosynthesis

The Biosynthesis of the Thiazole Moiety of Thiamin in the Archaeon <i>Halobacterium salinarum</i>

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