The biosynthetic route of the pyrimidine moiety of thiamin is different in prokaryotes and eukaryotes. In prokaryotes, the pyrimidine moiety is synthesized from aminoimidazole ribonucleotide, an intermediate of purine biosynthesis, while in eukaryotes, we have reported that the N-1, C-2, and N-3 atoms of the imidazole ring of histidine are incorporated into N-3, C-4, and the amino group attached to the C-4 atoms of the pyrimidine moiety, respectively, as a unit; the rest of the atoms of the pyrimidine moiety originate from pyridoxine as a unit. It has been reported that urocanic acid, the deaminated compound of histidine, is the direct precursor of the pyrimidine moiety. In the present report, we have investigated whether histidine or urocanic acid is the direct precursor of the pyrimidine moiety in Saccharomyces cerevisiae , using tracer experiments with 1) 13 C-formate and urocanic acid, 2) 15 N-NH 4 Cl and urocanic acid, 3) 15 N-NH 4 Cl and histidine, and 4) 13 C-histidine and urocanic acid. The GC-MS analysis revealed that the incorporation of the 15 N atom of 15 NH 4 Cl was not affected by the presence of urocanic acid, although it was affected by histidine, and the incorporation of 13 C-histidine was not affected by the presence of urocanic acid. These results confirm that histidine is the direct precursor of the pyrimidine moiety of thiamin in S. cerevisiae .
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.
The biosynthetic pathway of the pyrimidine moiety of thiamin was studied in the archaean Halobacterium salinarum. Thiamin is biosynthesized from 4-amino-5-hydroxymethyl-2-methylpyrimidine (pyrimidine) and 5-(2-hydroxyethyl)-4-methylthiazole (thiazole). The pyrimidine and the thiazole are biosynthesized de novo in microorganisms. The biosynthetic routes of pyrimidine in microorganisms differ between eukaryote and eubacteria. In the eukaryote Saccharomyces cerevisiae, histidine and pyridoxine are the precursors of pyrimidine, while in the eubacterium Escherichia coli, pyrimidine is biosynthesized from 5-aminoimidazole ribonucleotide (AIR), an intermediate of purine biosynthesis. Tracer investigations revealed that [(15)N]-, [1-(13)C]- and [2-(13)C] glycine, precursors of AIR, were incorporated into the pyrimidine in H. salinarum. These results suggested that the biosynthetic route of the pyrimidine in H. salinarum is similar to that of E. coli.
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