Precursor of carbon atom five and hydroxymethyl carbon atom of the pyrimidine moiety of thiamin in Escherichia coli.

Yamada, Kazuko; Kumaoka, Hiroshi

doi:10.3177/jnsv.29.389

Cited by 15 publications

(10 citation statements)

References 10 publications

(6 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…5), while the C2-N3 unit of this ring derives from the adjacent carbon and nitrogen atoms of glycine in Saccharomyces cerevisiae (6-8) or of tyrosine in Escherichia coli (9-11) and sulfur comes from cysteine (12)(13)(14). The pyrimidine moiety of vitamin B1 has been postulated to be derived from 5'-phosphoribosyl-5-aminoimidazole (15,16). The pyruvate dehydrogenase complex has been reported to be involved in the condensation of pyruvate and glyceraldehyde 3-phosphate (17, 18) to produce 1-deoxy-D-threo-2-pentulose.…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis of the thiazole moiety of thiamin (vitamin B1) in higher plant chloroplasts.

Julliard

Douce

1991

Proc. Natl. Acad. Sci. U.S.A.

123

View full text Add to dashboard Cite

The chloroplast stromal proteins from spinach condense the two heterocyclic moieties of vitamin B,-4-methyl-5-(J3-hydroxyethyl)thiazole and 2-methyl-4-amino-5-hydroxymethylpyrimidine-in the presence of MgATP. We have taken advantage of this observation to study thiazole synthesis. We present data indicating that pyruvate, glyceraldehyde 3-phosphate,-tyrosine, cysteine, and MgATP are required for this synthesis and that pyruvate and glyceraldehyde 3-phosphate can be replaced by 1-deoxy-D-threo-2-pentulose. The thiazole synthesis occurs at a sustained, low rate of 140 pmol per mg of protein per hr.It is remarkable that in 1990, more than half a century after the discovery and synthesis of vitamin B1 (1), the early biosynthetic steps of this important molecule remain obscure. The pathways have been studied by feeding microorganisms with small quantities of labeled precursors and accurately determinating the distribution of incorporated label. Nevertheless, the enzymes involved in the biosynthesis of the cyclic moieties of vitamin B1-2-methyl-4-amino-5-hydroxymethylpyrimidine and 4-methyl-5-(q-hydroxyethyl)thiazole-are still unknown.A 1-deoxy-D-threo-2-pentulose probably produced by the condensation of pyruvate and a triose phosphate has been proven to be the precursor of the contiguous five-carbon unit (C4'-C4-C5-C5'-C5") of the thiazole ring (refs. 2-4; however, see ref. 5), while the C2-N3 unit of this ring derives from the adjacent carbon and nitrogen atoms of glycine in Saccharomyces cerevisiae (6-8) or of tyrosine in Escherichia coli (9-11) and sulfur comes from cysteine (12)(13)(14). The pyrimidine moiety of vitamin B1 has been postulated to be derived from 5'-phosphoribosyl-5-aminoimidazole (15,16). The pyruvate dehydrogenase complex has been reported to be involved in the condensation of pyruvate and glyceraldehyde 3-phosphate (17, 18) to produce 1-deoxy-D-threo-2-pentulose.In higher plants, many enzyme-coenzyme complexes are unstable during purification. For example, highly purified preparations of pyruvate dehydrogenase from plant mitochondria are completely dependent on added thiamin pyrophosphate for enzymatic activity, but similar preparations of the mammalian enzymes show little or no response to exogenous thiamin pyrophosphate (19). If enzyme-coenzyme complexes are also unstable in vivo, the synthesis of vitamin B1 should be continuous and a significant rate of synthesis should be observed. Indirect evidence from mutants ofPisum sativum L. with altered pyrimidine moiety synthesis (20) shows that a high level of exogenous thiamin is required in order to restore normal cellular metabolism. Nevertheless, the biosynthetic pathways of the pyrimidine and thiazole rings of vitamin B1 in higher plants are totally unexplored.Here, we report evidence that the chloroplast is a site for the synthesis of the thiazole moiety of vitamin B1, which derives from 1-deoxy-D-threo-2-pentulose, tyrosine, and cysteine. MATERIALS AND METHODS Preparation of Soluble (Stromal) Proteins from Spinach LeafChloroplasts. Al...

show abstract

Section: Introductionmentioning

confidence: 99%

Biosynthesis of the thiazole moiety of thiamin (vitamin B1) in higher plant chloroplasts.

Julliard

Douce

1991

Proc. Natl. Acad. Sci. U.S.A.

123

View full text Add to dashboard Cite

show abstract

“…1. Radiotracing studies determined that carbon from AIR is incorporated into thiamine and, furthermore, that all the carbons in the pyrimidine moiety of thiamine are derived from AIR (9,28,29). In addition, [14C]formate and [14C]glycine (precursors of the purines) were incorporated into the pyrimidine moiety, indicating that the source of AIR was de novo purine biosynthesis (10).…”

mentioning

confidence: 99%

Evidence for a new, oxygen-regulated biosynthetic pathway for the pyrimidine moiety of thiamine in Salmonella typhimurium

Downs

1992

J Bacteriol

View full text Add to dashboard Cite

The synthesis of the pyrimidine moiety of thiamine (vitamin B1) shares five reactions with the de novo purine biosynthetic pathway. Aminoimidazole ribotide (AIR) is the last common intermediate before the two pathways diverge. Evidence for the existence of a new pathway to the pyrimidine which bypasses the de novo purine biosynthetic pathway is reported here. This pathway is only expressed under anaerobic growth conditions and is denoted alternative pyrimidine biosynthesis or APB. Labeling studies are consistent with pantothenate being a precursor to the pyrimidine moiety of thiamine that is synthesized by the APB pathway. The APB pathway is independent of the alternative purF function which was proposed previously (D. M. Downs and J. R. Roth, J. Bacteriol. 173:6597-6604, 1991). The alternative purF function is shown here to be affected by temperature and exogenous pantothenate. Although the evidence suggests that the APB pathway is separate from the alternative purF function, the relationship between this function and the APB pathway is not yet clear.

show abstract

“…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%

“…In prokaryotes, the pyrimidine is synthesized from 5-aminoimidazole ribonucleotide (AIR), an intermediate of purine biosynthesis (7)(8)(9). The pyrimidine is formed by ring expansion of imidazole with the insertion of the C-4′, C-5′ fragment of the ribose residue of AIR (10,11). In eukaryotes, we have shown that the N-3, C-4 and amino-N atoms of the pyrimidine are derived from the N-1, C-2 and N-3 atoms of the imidazole ring of histidine as a unit (12,13), while a unit consisting of C-2′, C-2, N-1, C-6, C-5 and C-5′ from pyridoxine is incorporated into the same location in the pyrimidine (14,15).…”

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

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Precursor of carbon atom five and hydroxymethyl carbon atom of the pyrimidine moiety of thiamin in Escherichia coli.

Cited by 15 publications

References 10 publications

Biosynthesis of the thiazole moiety of thiamin (vitamin B1) in higher plant chloroplasts.

Biosynthesis of the thiazole moiety of thiamin (vitamin B1) in higher plant chloroplasts.

Evidence for a new, oxygen-regulated biosynthetic pathway for the pyrimidine moiety of thiamine in Salmonella typhimurium

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

Contact Info

Product

Resources

About