The thiJ locus and its relation to phosphorylation of hydroxymethyl pyrimidine in Escherichia coli
Tomoko Mizote, Masataka Tsuda, Teruko Nakazawa, Hideo Nakayama
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.
https://doi.org/10.1099/13500872-142-10-2969
Published - 1996 Oct
Hydroxymethylpyrimidine
Thiamin biosynthesis
thiJ locus
10.1099/13500872-142-10-2969
Dive into the research topics of 'The thiJ locus and its relation to phosphorylation of hydroxymethyl pyrimidine in Escherichia coli'. Together they form a unique fingerprint.
hydroxymethylpyrimidine kinase Medicine & Life Sciences 100%
phosphomethylpyrimidine kinase Medicine & Life Sciences 67%
hydroxyethylthiazole kinase Medicine & Life Sciences 64%
pyrimidine Medicine & Life Sciences 53%
Escherichia coli Medicine & Life Sciences 30%
Phosphorylation Medicine & Life Sciences 30%
Pyridoxal Kinase Medicine & Life Sciences 26%
Mizote, T., Tsuda, M., Nakazawa, T., & Nakayama, H. (1996). The thiJ locus and its relation to phosphorylation of hydroxymethyl pyrimidine in Escherichia coli. Microbiology, 142(10), 2969-2974. https://doi.org/10.1099/13500872-142-10-2969
The thiJ locus and its relation to phosphorylation of hydroxymethyl pyrimidine in Escherichia coli. / Mizote, Tomoko; Tsuda, Masataka; Nakazawa, Teruko; Nakayama, Hideo.
In: Microbiology, Vol. 142, No. 10, 10.1996, p. 2969-2974.
Mizote, T, Tsuda, M, Nakazawa, T & Nakayama, H 1996, 'The thiJ locus and its relation to phosphorylation of hydroxymethyl pyrimidine in Escherichia coli', Microbiology, vol. 142, no. 10, pp. 2969-2974. https://doi.org/10.1099/13500872-142-10-2969
Mizote T, Tsuda M, Nakazawa T, Nakayama H. The thiJ locus and its relation to phosphorylation of hydroxymethyl pyrimidine in Escherichia coli. Microbiology. 1996 Oct;142(10):2969-2974. https://doi.org/10.1099/13500872-142-10-2969
Mizote, Tomoko ; Tsuda, Masataka ; Nakazawa, Teruko ; Nakayama, Hideo. / The thiJ locus and its relation to phosphorylation of hydroxymethyl pyrimidine in Escherichia coli. In: Microbiology. 1996 ; Vol. 142, No. 10. pp. 2969-2974.
@article{624cccf81fd94a799c5037161b672b4e,
title = "The thiJ locus and its relation to phosphorylation of hydroxymethyl pyrimidine in Escherichia coli",
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.",
keywords = "Escherichia coli, Hydroxymethylpyrimidine, Thiamin biosynthesis, thiJ locus",
author = "Tomoko Mizote and Masataka Tsuda and Teruko Nakazawa and Hideo Nakayama",
doi = "10.1099/13500872-142-10-2969",
journal = "Microbiology (Reading, England)",
publisher = "Society for General Microbiology",
T1 - The thiJ locus and its relation to phosphorylation of hydroxymethyl pyrimidine in Escherichia coli
AU - Mizote, Tomoko
AU - Tsuda, Masataka
AU - Nakazawa, Teruko
AU - Nakayama, Hideo
N2 - 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.
AB - 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.
KW - Escherichia coli
KW - Hydroxymethylpyrimidine
KW - Thiamin biosynthesis
KW - thiJ locus
U2 - 10.1099/13500872-142-10-2969
DO - 10.1099/13500872-142-10-2969
JO - Microbiology (Reading, England)
JF - Microbiology (Reading, England)