The thiJ locus and its relation to phosphorylation of hydroxymethyl pyrimidine in Escherichia coli

Tomoko Mizote, Masataka Tsuda, Teruko Nakazawa, Hideo Nakayama

    Research output: Contribution to journalArticle

    17 Citations (Scopus)

    Abstract

    Extracts from Escherichia coli K-12 contained two distinct enzymes capable of catalysing the phosphorylation of hydroxymethylpyrimidine (HMP) to HMP monophosphate: pyridoxine kinase (EC 2.7.1.35) and an enzyme that has not previously been genetically analysed, HMP kinase (EC 2.7.1.49). Two distinct genes, pdxL and thiJ, specify the activities of the former and latter enzymes, respectively. The inactivation of both genes by independent mutations in the same cell resulted in the complete loss of HMP kinase activity. Experiments with a series of strains that carry mutations in thiC, thiC pdxB, thiC pdxB pdxL and thiC pdxB pdxL thiJ revealed that the ability of the double mutant (pdxL thiJ) to utilize HMP in thiamin pyrophosphate biosynthesis was restored by introducing the wild-type allele corresponding to the thiJ mutation. The thiJ locus was mapped on the chromosome near the thiD and thiM loci, which govern the activities of phosphomethylpyrimidine kinase (EC 2.7.4.7) and hydroxyethylthiazole kinase (EC 2.7.1.50), respectively.

    Original languageEnglish
    Pages (from-to)2969-2974
    Number of pages6
    JournalMicrobiology
    Volume142
    Issue number10
    DOIs
    Publication statusPublished - 1996 Oct

    Keywords

    • Escherichia coli
    • Hydroxymethylpyrimidine
    • Thiamin biosynthesis
    • thiJ locus

    ASJC Scopus subject areas

    • Microbiology

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