Thiamine pyrophosphokinase

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Thiamine pyrophosphokinase

Existing structural data : 1oly

Properties of human protein
Mass / length primary structure 243 amino acids
Secondary to quaternary structure Homodimer
Cofactor magnesium
Identifier
Gene name TPK1
External IDs
Enzyme classification
EC, category 2.7.6.2 kinase
Response type Transfer of pyrophosphate
Substrate ATP + thiamine
Products AMP + thiamine pyrophosphate
Occurrence
Homology family TPK
Parent taxon Eukaryotes

Thiaminpyrophosphokinase (TPK) is the enzyme that catalyzes the conversion of thiamine (vitamin B1) in thiamine pyrophosphate (TPP) catalyzes . This phosphorylation is necessary because thiamine itself has no use in metabolism. TPK occurs in all eukaryotes , in humans it is particularly localized in the heart , kidneys , testes , small intestine and leukocytes .

Variants of the enzyme may be associated with differences in birth weight. The regulation of TPK takes place via the Sp1 cis element .

Catalyzed reaction

B1+ ATP   + AMP  TPP

Thiamine is phosphorylated to TPP. Magnesium is necessary as a cofactor. Also pyrithiamine is accepted as a substrate.

Individual evidence

  1. a b UniProt Q9H3S4
  2. Fradin D, Bougneres P: Three common intronic variants in the maternal and fetal thiamine pyrophosphokinase gene (TPK1) are associated with birth weight . In: Ann. Hum. Genet. . 71, No. Pt 5, September 2007, pp. 578-85. doi : 10.1111 / j.1469-1809.2007.00348.x . PMID 17295612 .
  3. Onozuka M, Konno H, Akaji K, Nishino H, Nosaka K: Molecular cloning and analysis of the 5'-flanking region of the human thiamine pyrophosphokinase gene . In: J. Nutr. Sci. Vitaminol. . 51, No. 4, August 2005, pp. 274-7. PMID 16262001 .

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