Thiamine monophosphate

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Thiamine monophosphate
Thiamine monophosphate.svg
Identifiers
3D model (JSmol)
ChEBI
ChemSpider
ECHA InfoCard 100.007.762 OOjs UI icon edit-ltr-progressive.svg
MeSH Thiamine+Monophosphate
PubChem CID
UNII
  • InChI=1S/C12H17N4O4PS.ClH/c1-8-11(3-4-20-21(17,18)19)22-7-16(8)6-10-5-14-9(2)15-12(10)13;/h5,7H,3-4,6H2,1-2H3,(H3-,13,14,15,17,18,19);1H Yes check.svgY
    Key: GUGWNSHJDUEHNJ-UHFFFAOYSA-N Yes check.svgY
  • InChI=1/C12H17N4O4PS.ClH/c1-8-11(3-4-20-21(17,18)19)22-7-16(8)6-10-5-14-9(2)15-12(10)13;/h5,7H,3-4,6H2,1-2H3,(H3-,13,14,15,17,18,19);1H
    Key: GUGWNSHJDUEHNJ-UHFFFAOYAK
  • Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCOP(=O)(O)O.[Cl-]
Properties
C12H18N4O4PS+
Molar mass 345.336 g/mol
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
X mark.svgN  verify  (what is  Yes check.svgYX mark.svgN ?)

Thiamine monophosphate, also known as ThMP and TMP, is a phosphate ester of thiamine. [1]

It is an intermediate from the hydrolysis of thiamine diphosphate to free thiamine by alkaline phosphatase. [2] [3] [4] The conversion of ThMP to thiamine cannot be facilitated by acid hydrolysis. [5] ThMP is also enzymatically synthesized by thiamine-phosphate pyrophosphorylase, which combines thiazole in its monophosphate form and pyrimidine as a pyrophosphate. [6]

The physiological function of ThMP has not been identified. [2]

Physiological presence

In whole human blood, both ThMP and free thiamine are present in lower concentrations as compared to TPP, but they are found in low amounts in plasma. [4] ThMP is the only phosphorylated thiamine derivative found in human cerebral spinal fluid. [4] [7]

It occurs naturally in bovine milk. [8]

In rats, approximately 64% of the total thiamine in plasma exists in its the monophosphate form. [9] After injection of ThMP into the femoral vein of rats, it was quickly transported to the cerebral tissue without chemical modification, but the average transport rate was 5-10 times slower than that of thiamine. [10]

Related Research Articles

<span class="mw-page-title-main">Nucleotide</span> Biological molecules constituting nucleic acids

Nucleotides are organic molecules composed of a nitrogenous base, a pentose sugar and a phosphate. They serve as monomeric units of the nucleic acid polymers – deoxyribonucleic acid (DNA) and ribonucleic acid (RNA), both of which are essential biomolecules within all life-forms on Earth. Nucleotides are obtained in the diet and are also synthesized from common nutrients by the liver.

<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">Pyrophosphate</span> Class of chemical compounds

In chemistry, pyrophosphates are phosphorus oxyanions that contain two phosphorus atoms in a P−O−P linkage. A number of pyrophosphate salts exist, such as disodium pyrophosphate and tetrasodium pyrophosphate, among others. Often pyrophosphates are called diphosphates. The parent pyrophosphates are derived from partial or complete neutralization of pyrophosphoric acid. The pyrophosphate bond is also sometimes referred to as a phosphoanhydride bond, a naming convention which emphasizes the loss of water that occurs when two phosphates form a new P−O−P bond, and which mirrors the nomenclature for anhydrides of carboxylic acids. Pyrophosphates are found in ATP and other nucleotide triphosphates, which are important in biochemistry. The term pyrophosphate is also the name of esters formed by the condensation of a phosphorylated biological compound with inorganic phosphate, as for dimethylallyl pyrophosphate. This bond is also referred to as a high-energy phosphate bond.

In organic chemistry, a tetrose is a monosaccharide with 4 carbon atoms. They have either an aldehyde functional group in position 1 (aldotetroses) or a ketone group in position 2 (ketotetroses).

A nucleoside triphosphate is a nucleoside containing a nitrogenous base bound to a 5-carbon sugar, with three phosphate groups bound to the sugar. They are the molecular precursors of both DNA and RNA, which are chains of nucleotides made through the processes of DNA replication and transcription. Nucleoside triphosphates also serve as a source of energy for cellular reactions and are involved in signalling pathways.

<span class="mw-page-title-main">Transketolase</span> Enzyme involved in metabolic pathways

Transketolase is an enzyme that, in humans, is encoded by the TKT gene. It participates in both the pentose phosphate pathway in all organisms and the Calvin cycle of photosynthesis. Transketolase catalyzes two important reactions, which operate in opposite directions in these two pathways. In the first reaction of the non-oxidative pentose phosphate pathway, the cofactor thiamine diphosphate accepts a 2-carbon fragment from a 5-carbon ketose (D-xylulose-5-P), then transfers this fragment to a 5-carbon aldose (D-ribose-5-P) to form a 7-carbon ketose (sedoheptulose-7-P). The abstraction of two carbons from D-xylulose-5-P yields the 3-carbon aldose glyceraldehyde-3-P. In the Calvin cycle, transketolase catalyzes the reverse reaction, the conversion of sedoheptulose-7-P and glyceraldehyde-3-P to pentoses, the aldose D-ribose-5-P and the ketose D-xylulose-5-P.

<span class="mw-page-title-main">Purine nucleoside phosphorylase</span> Enzyme

Purine nucleoside phosphorylase, PNP, PNPase or inosine phosphorylase is an enzyme that in humans is encoded by the NP gene. It catalyzes the chemical reaction

<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">GMP synthase</span>

Guanosine monophosphate synthetase, also known as GMPS is an enzyme that converts xanthosine monophosphate to guanosine monophosphate.

dCMP deaminase Protein-coding gene in the species Homo sapiens

dCMP deaminase is an enzyme which converts deoxycytidylic acid to deoxyuridylic acid.

<span class="mw-page-title-main">Inositol-phosphate phosphatase</span> Class of enzymes

The enzyme Inositol phosphate-phosphatase is of the phosphodiesterase family of enzymes. It is involved in the phosphophatidylinositol signaling pathway, which affects a wide array of cell functions, including but not limited to, cell growth, apoptosis, secretion, and information processing. Inhibition of inositol monophosphatase may be key in the action of lithium in treating bipolar disorder, specifically manic depression.

<span class="mw-page-title-main">Adenosine 3',5'-bisphosphate</span> Chemical compound

Adenosine 3',5'-bisphosphate is a form of an adenosine nucleotide with two phosphate groups attached to different carbons in the ribose ring. This is distinct from adenosine diphosphate, where the two phosphate groups are attached in a chain to the 5' carbon atom in the ring.

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

In enzymology, a nucleoside-phosphate kinase is an enzyme that catalyzes the chemical reaction

In enzymology, a thiamine-diphosphate kinase is an enzyme involved in thiamine metabolism. It catalyzes the chemical reaction

In enzymology, a thiamine kinase is an enzyme that catalyzes the chemical reaction

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

<span class="mw-page-title-main">Inosine-5′-monophosphate dehydrogenase</span> Class of enzymes

Inosine-5′-monophosphate dehydrogenase (IMPDH) is a purine biosynthetic enzyme that catalyzes the nicotinamide adenine dinucleotide (NAD+)-dependent oxidation of inosine monophosphate (IMP) to xanthosine monophosphate (XMP), the first committed and rate-limiting step towards the de novo biosynthesis of guanine nucleotides from IMP. IMPDH is a regulator of the intracellular guanine nucleotide pool, and is therefore important for DNA and RNA synthesis, signal transduction, energy transfer, glycoprotein synthesis, as well as other process that are involved in cellular proliferation.

<span class="mw-page-title-main">Thymidylate kinase</span>

Thymidylate kinase catalyzes the phosphorylation of thymidine 5'-monophosphate (dTMP) to form thymidine 5'-diphosphate (dTDP) in the presence of ATP and magnesium:

<span class="mw-page-title-main">Leloir pathway</span>

The Leloir pathway is a metabolic pathway for the catabolism of D-galactose. It is named after Luis Federico Leloir, who first described it.

References

  1. Mancinelli R, Ceccanti M, Guiducci MS, Sasso GF, Sebastiani G, Attilia ML, et al. (June 2003). "Simultaneous liquid chromatographic assessment of thiamine, thiamine monophosphate and thiamine diphosphate in human erythrocytes: a study on alcoholics". Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences. 789 (2): 355–363. doi:10.1016/S1570-0232(03)00139-9. PMID   12742126.
  2. 1 2 Lonsdale D (2018). "Thiamin". Advances in Food and Nutrition Research. 83. Elsevier: 1–56. doi:10.1016/bs.afnr.2017.11.001. ISBN   978-0-12-811803-0. PMID   29477220.
  3. Lonsdale D, Marrs C (January 2017). "Chapter 3 - Mitochondria, Thiamine, and Autonomic Dysfunction". In Lonsdale D, Marrs C (eds.). Thiamine Deficiency Disease, Dysautonomia, and High Calorie Malnutrition. Academic Press. pp. 59–103. doi:10.1016/b978-0-12-810387-6.00003-4. ISBN   978-0-12-810387-6.
  4. 1 2 3 Gangolf M, Czerniecki J, Radermecker M, Detry O, Nisolle M, Jouan C, et al. (October 2010). German M (ed.). "Thiamine status in humans and content of phosphorylated thiamine derivatives in biopsies and cultured cells". PLOS ONE. 5 (10): e13616. Bibcode:2010PLoSO...513616G. doi: 10.1371/journal.pone.0013616 . PMC   2963613 . PMID   21049048.
  5. Burch HB, Bessey OA, Love RH, Lowry OH (September 1952). "The determination of thiamine and thiamine phosphates in small quantities of blood and blood cells". The Journal of Biological Chemistry. 198 (1): 477–490. doi: 10.1016/s0021-9258(18)55601-5 . PMID   12999762.
  6. Leder IG (November 1961). "The enzymatic synthesis of thiamine monophosphate". The Journal of Biological Chemistry. 236 (11): 3066–3071. doi: 10.1016/s0021-9258(19)76430-8 . PMID   14463407.
  7. Rindi G, Patrini C, Poloni M (September 1981). "Monophosphate, the only phosphoric ester of thiamin in the cerebro-spinal fluid". Experientia. 37 (9): 975–976. doi:10.1007/BF01971788. PMID   7297660.
  8. Schmidt A, Pratsch H, Schreiner MG, Mayer HK (August 2017). "Determination of the native forms of vitamin B1 in bovine milk using a fast and simplified UHPLC method". Food Chemistry. 229: 452–457. doi:10.1016/j.foodchem.2017.02.092. PMID   28372200.
  9. Rindi G, De Giuseppe L, Sciorelli G (April 1968). "Thiamine monophosphate, a normal constituent of rat plasma". The Journal of Nutrition. 94 (4): 447–454. doi:10.1093/jn/94.4.447. PMID   4297480.
  10. Reggiani C, Patrini C, Rindi G (February 1984). "Nervous tissue thiamine metabolism in vivo. I. Transport of thiamine and thiamine monophosphate from plasma to different brain regions of the rat". Brain Research. 293 (2): 319–327. doi:10.1016/0006-8993(84)91239-3. PMID   6697223.