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. 1988 Oct;88(2):248–250. doi: 10.1104/pp.88.2.248

A th-1 Mutant of Arabidopsis thaliana Is Defective for a Thiamin-Phosphate-Synthesizing Enzyme: Thiamin Phosphate Pyrophosphorylase 1

Yoshibumi Komeda 1,2, Miyako Tanaka 1,2, Takahiro Nishimune 1,2
PMCID: PMC1055562  PMID: 16666289

Abstract

We have examined the activity of the thiamin phosphate pyrophosphorylase in Arabidopsis thaliana wild type and in a mutant (th-1) which requires exogenous thiamin for growth. Mutant and wild-type plants grown in 1 × 10−7 molar thiamin were used for the examination of the production of thiamin and thiamin monophosphate (TMP) using 4-methyl-5-hydroxyethylthiazole phosphate and 2-methyl-4-amino-5-hydroxymethylpyrimidine pyrophosphate as substrates. While the wild-type strain formed both thiamin and TMP, the th-1 mutant did not. When TMP was added to the extracts, the th-1 mutant, as well as wild type, produced thiamin. Accordingly, it was concluded that the th-1 mutant was defective in the activity of TMP pyrophosphorylase. Some of the characteristics of the enzyme from the wild-type plant were examined. The optimum temperature for the reaction is 45°C, and the Km values for the substrates are 2.7 × 10−6 molar for 4-methyl-5-hydroxyethylthiazole phosphate and 1.8 × 10−6 molar for 2-methyl-4-amino-5-hydroxymethylpyrimidine pyrophosphate.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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