Thiazole synthase

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Thiazole synthase
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Thiazole synthase oktamer, Saccharomyces cerevisiae
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EC no. 2.8.1.10
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Thiazole synthase (EC 2.8.1.10, thiG (gene)) is an enzyme with systematic name 1-deoxy-D-xylulose 5-phosphate:thiol sulfurtransferase. [1] [2] [3] [4] [5] [6] This enzyme catalyses the following chemical reaction

1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS] 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O

H2S can provide the sulfur in vitro.

Related Research Articles

<span class="mw-page-title-main">Thiamine</span> Chemical compound

Thiamine, also known as thiamin and vitamin B1, is a vitamin, an essential micronutrient for humans and animals. It is found in food and commercially synthesized to be a dietary supplement or medication. Phosphorylated forms of thiamine are required for some metabolic reactions, including the breakdown of glucose and amino acids.

<span class="mw-page-title-main">Thiaminase</span> Class of enzymes

Thiaminase is an enzyme that metabolizes or breaks down thiamine into two molecular parts. It is an antinutrient when consumed.

<span class="mw-page-title-main">Phosphoribosyl pyrophosphate</span> Chemical compound

Phosphoribosyl pyrophosphate (PRPP) is a pentose phosphate. It is a biochemical intermediate in the formation of purine nucleotides via inosine-5-monophosphate, as well as in pyrimidine nucleotide formation. Hence it is a building block for DNA and RNA. The vitamins thiamine and cobalamin, and the amino acid tryptophan also contain fragments derived from PRPP. It is formed from ribose 5-phosphate (R5P) by the enzyme ribose-phosphate diphosphokinase:

<span class="mw-page-title-main">Phosphoribosylamine</span> Chemical compound

Phosphoribosylamine (PRA) is a biochemical intermediate in the formation of purine nucleotides via inosine-5-monophosphate, and hence is a building block for DNA and RNA. The vitamins thiamine and cobalamin also contain fragments derived from PRA.

<span class="mw-page-title-main">Phosphoribosyl-N-formylglycineamide</span> Chemical compound

Phosphoribosyl-N-formylglycineamide is a biochemical intermediate in the formation of purine nucleotides via inosine-5-monophosphate, and hence is a building block for DNA and RNA. The vitamins thiamine and cobalamin also contain fragments derived from FGAR.

In enzymology, a 1-deoxy-d-xylulose-5-phosphate synthase (EC 2.2.1.7) is an enzyme in the non-mevalonate pathway that catalyzes the chemical reaction

<span class="mw-page-title-main">Pyridoxine 5'-phosphate synthase</span> Class of enzymes

In enzymology, a pyridoxine 5'-phosphate synthase (EC 2.6.99.2) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">5-Aminoimidazole ribotide</span> Chemical compound

5′-Phosphoribosyl-5-aminoimidazole is a biochemical intermediate in the formation of purine nucleotides via inosine-5-monophosphate, and hence is a building block for DNA and RNA. The vitamins thiamine and cobalamin also contain fragments derived from AIR. It is an intermediate in the adenine pathway and is synthesized from 5′-phosphoribosylformylglycinamidine by AIR synthetase.

<span class="mw-page-title-main">5′-Phosphoribosylformylglycinamidine</span> Chemical compound

5′-Phosphoribosylformylglycinamidine is a biochemical intermediate in the formation of purine nucleotides via inosine-5-monophosphate, and hence is a building block for DNA and RNA. The vitamins thiamine and cobalamin also contain fragments derived from FGAM.

<span class="mw-page-title-main">Glycineamide ribonucleotide</span> Chemical compound

Glycineamide ribonucleotide is a biochemical intermediate in the formation of purine nucleotides via inosine-5-monophosphate, and hence is a building block for DNA and RNA. The vitamins thiamine and cobalamin also contain fragments derived from GAR.

Molybdopterin synthase (EC 2.8.1.12, MPT synthase) is an enzyme required to synthesize molybdopterin (MPT) from precursor Z (now known as cyclic pyranopterin monophosphate). Molydopterin is subsequently complexed with molybdenum to form molybdenum cofactor (MoCo). MPT synthase catalyses the following chemical reaction:

Radical SAM is a designation for a superfamily of enzymes that use a [4Fe-4S]+ cluster to reductively cleave S-adenosyl-L-methionine (SAM) to generate a radical, usually a 5′-deoxyadenosyl radical (5'-dAdo), as a critical intermediate. These enzymes utilize this radical intermediate to perform diverse transformations, often to functionalize unactivated C-H bonds. Radical SAM enzymes are involved in cofactor biosynthesis, enzyme activation, peptide modification, post-transcriptional and post-translational modifications, metalloprotein cluster formation, tRNA modification, lipid metabolism, biosynthesis of antibiotics and natural products etc. The vast majority of known radical SAM enzymes belong to the radical SAM superfamily, and have a cysteine-rich motif that matches or resembles CxxxCxxC. rSAMs comprise the largest superfamily of metal-containing enzymes.

2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase is an enzyme with systematic name L-aspartate 4-semialdehyde:1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate methylglyoxaltransferase. This enzyme catalyses the following chemical reaction

Sulfur carrier protein ThiS adenylyltransferase is an enzyme with systematic name ATP:(ThiS) adenylyltransferase. This enzyme catalyses the following chemical reaction

Molybdopterin synthase sulfurtransferase is an enzyme with systematic name persulfurated L-cysteine desulfurase:(molybdopterin-synthase sulfur-carrier protein)-Gly-Gly sulfurtransferase. This enzyme catalyses the following chemical reaction

Aminopyrimidine aminohydrolase (EC 3.5.99.2, thiaminase, thiaminase II, tenA (gene)) is an enzyme with systematic name 4-amino-5-aminomethyl-2-methylpyrimidine aminohydrolase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Phosphomethylpyrimidine synthase</span>

Phosphomethylpyrimidine synthase is an enzyme with systematic name 5-amino-1-(5-phospho-D-ribosyl)imidazole formate-lyase . This enzyme catalyses the following chemical reaction

Pyridoxal 5′-phosphate synthase (glutamine hydrolysing) (EC 4.3.3.6, PdxST) is an enzyme with systematic name D-ribose 5-phosphate,D-glyceraldehyde 3-phosphate pyridoxal 5′-phosphate-lyase. This enzyme catalyses the following chemical reaction

Thiazole tautomerase is an enzyme with systematic name 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate isomerase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">4-Amino-5-hydroxymethyl-2-methylpyrimidine</span> Chemical compound

Within the field of biochemistry, 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) also known as toxopyrimidine together with its mono phosphate (HMP-P) and pyrophosphate (HMP-PP) esters are biogenetic precursors to the important biochemical cofactor thiamine pyrophosphate (TPP), a derivative of thiamine (vitamin B1).

References

  1. Park JH, Dorrestein PC, Zhai H, Kinsland C, McLafferty FW, Begley TP (October 2003). "Biosynthesis of the thiazole moiety of thiamin pyrophosphate (vitamin B1)". Biochemistry. 42 (42): 12430–8. doi:10.1021/bi034902z. PMID   14567704.
  2. Dorrestein PC, Zhai H, McLafferty FW, Begley TP (October 2004). "The biosynthesis of the thiazole phosphate moiety of thiamin: the sulfur transfer mediated by the sulfur carrier protein ThiS". Chemistry & Biology. 11 (10): 1373–81. doi: 10.1016/j.chembiol.2004.08.009 . PMID   15489164.
  3. Dorrestein PC, Zhai H, Taylor SV, McLafferty FW, Begley TP (March 2004). "The biosynthesis of the thiazole phosphate moiety of thiamin (vitamin B1): the early steps catalyzed by thiazole synthase". Journal of the American Chemical Society. 126 (10): 3091–6. doi:10.1021/ja039616p. PMID   15012138.
  4. Settembre EC, Dorrestein PC, Zhai H, Chatterjee A, McLafferty FW, Begley TP, Ealick SE (September 2004). "Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole synthase/sulfur carrier protein complex". Biochemistry. 43 (37): 11647–57. doi:10.1021/bi0488911. PMID   15362849.
  5. Hazra A, Chatterjee A, Begley TP (March 2009). "Biosynthesis of the thiamin thiazole in Bacillus subtilis: identification of the product of the thiazole synthase-catalyzed reaction". Journal of the American Chemical Society. 131 (9): 3225–9. doi:10.1021/ja806752h. PMC   2765510 . PMID   19216519.
  6. Hazra AB, Han Y, Chatterjee A, Zhang Y, Lai RY, Ealick SE, Begley TP (June 2011). "A missing enzyme in thiamin thiazole biosynthesis: identification of TenI as a thiazole tautomerase". Journal of the American Chemical Society. 133 (24): 9311–9. doi:10.1021/ja1110514. PMC   3116082 . PMID   21534620.