Aminopyrimidine aminohydrolase

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Aminopyrimidine aminohydrolase
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EC no. 3.5.99.2
CAS no. 9024-80-0
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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. [1] [2] [3] [4] [5] [6] [7] This enzyme catalyses the following chemical reaction

(1) 4-amino-5-aminomethyl-2-methylpyrimidine + H2O 4-amino-5-hydroxymethyl-2-methylpyrimidine + ammonia
(2) thiamine + H2O 4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole

This enzyme was previously known as thiaminase II.

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.

In enzymology, a thiamine oxidase (EC 1.1.3.23) is an enzyme that catalyzes the chemical reaction

In enzymology, a dCTP deaminase (EC 3.5.4.13) is an enzyme that catalyzes the chemical reaction

In enzymology, a thiamine-phosphate diphosphorylase is an enzyme that catalyzes the chemical reaction

In enzymology, a hydroxymethylpyrimidine kinase 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.

FAD-dependent urate hydroxylase is an enzyme with systematic name urate,NADH:oxygen oxidoreductase . A non-homologous isofunctional enzyme (NISE) to HpxO was found, and named HpyO. HpyO was determined to be a typical Michaelian enzyme. These FAD-dependent urate hydroxylases are flavoproteins.

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

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

Thiazole synthase (EC 2.8.1.10, thiG (gene)) is an enzyme with systematic name 1-deoxy-D-xylulose 5-phosphate:thiol sulfurtransferase. This enzyme catalyses the following chemical reaction

Methylenediurea deaminase (EC 3.5.3.21, methylenediurease) is an enzyme with systematic name methylenediurea aminohydrolase found in Brucella anthropi, a bacterium. This enzyme catalyses the following chemical reaction:

<span class="mw-page-title-main">6-carboxytetrahydropterin synthase</span> Enzyme

6-carboxytetrahydropterin synthase (EC 4.1.2.50, CPH4 synthase, queD (gene), ToyB, ykvK (gene)) is an enzyme with systematic name 7,8-dihydroneopterin 3'-triphosphate acetaldehyde-lyase (6-carboxy-5,6,7,8-tetrahydropterin and triphosphate-forming). This enzyme catalyses the following reversible 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. Fujita A, Nose Y (July 1954). "The second type of bacterial thiaminase". The Journal of Vitaminology. 1 (1): 1–7. doi: 10.5925/jnsv1954.1.1 . PMID   13243520.
  2. Ikehata H (1960). "Purification of thiaminase II". J. Gen. Appl. Microbiol. 6: 30–39. doi: 10.2323/jgam.6.30 .
  3. Toms AV, Haas AL, Park JH, Begley TP, Ealick SE (February 2005). "Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II". Biochemistry. 44 (7): 2319–29. doi:10.1021/bi0478648. PMID   15709744.
  4. Benach J, Edstrom WC, Lee I, Das K, Cooper B, Xiao R, Liu J, Rost B, Acton TB, Montelione GT, Hunt JF (May 2005). "The 2.35 A structure of the TenA homolog from Pyrococcus furiosus supports an enzymatic function in thiamine metabolism". Acta Crystallographica Section D. 61 (Pt 5): 589–98. doi:10.1107/S0907444905005147. PMID   15858269.
  5. Jenkins AH, Schyns G, Potot S, Sun G, Begley TP (August 2007). "A new thiamin salvage pathway". Nature Chemical Biology. 3 (8): 492–7. doi:10.1038/nchembio.2007.13. PMID   17618314.
  6. Jenkins AL, Zhang Y, Ealick SE, Begley TP (February 2008). "Mutagenesis studies on TenA: a thiamin salvage enzyme from Bacillus subtilis". Bioorganic Chemistry. 36 (1): 29–32. doi:10.1016/j.bioorg.2007.10.005. PMC   2293645 . PMID   18054064.
  7. French JB, Begley TP, Ealick SE (September 2011). "Structure of trifunctional THI20 from yeast". Acta Crystallographica Section D. 67 (Pt 9): 784–91. doi:10.1107/S0907444911024814. PMC   3169313 . PMID   21904031.