Molecular cloning of human thiamin pyrophosphokinase

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Thiamin pyrophosphokinase (TPK, EC 2.7.6.2) catalyses phosphorylation of thiamin to thiamin pyrophosphate, an active enzyme cofactor. Here we describe the cloning of complete human TPK1 cDNA from an adult liver library. Human TPK1 is 89% identical to murine TPK1 at the protein level. The gene maps to chromosome 7q34-36, consists of at least eight exons, and spans a distance at least of 420 kb. The mRNA of human TPK1 is highly expressed in testis, small intestine and kidney with lesser but detectable expression in brain, liver, placenta and spleen. The availability of the human TPK1 gene will provide another useful tool for studying the role of this enzyme in human thiamin metabolism and deficiency state.

Original languageEnglish (US)
Pages (from-to)320-322
Number of pages3
JournalBiochimica et Biophysica Acta - Gene Structure and Expression
Volume1517
Issue number2
DOIs
StatePublished - Jan 26 2001

Fingerprint

Thiamin Pyrophosphokinase
Cloning
Thiamine
Molecular Cloning
Liver
Genes
Thiamine Pyrophosphate
Phosphorylation
Coenzymes
Chromosomes
Metabolism
Exons
Brain
Complementary DNA
Availability
Thiamine Deficiency
Messenger RNA
Enzymes
Placenta
Small Intestine

Keywords

  • Cofactor
  • Pyrophosphate
  • Pyrophosphokinase
  • Thiamin

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Structural Biology
  • Biophysics

Cite this

Molecular cloning of human thiamin pyrophosphokinase. / Zhao, Rongbao; Gao, Feng; Goldman, I. David.

In: Biochimica et Biophysica Acta - Gene Structure and Expression, Vol. 1517, No. 2, 26.01.2001, p. 320-322.

Research output: Contribution to journalArticle

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