Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation

S. V. Taylor; N. L. Kelleher; C. Kinsland; H. J. Chiu; C. A. Costello; A. D. Backstrom; F. W. McLafferty; T. P. Begley

doi:10.1074/jbc.273.26.16555

Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation

S. V. Taylor, N. L. Kelleher, C. Kinsland, H. J. Chiu, C. A. Costello, A. D. Backstrom, F. W. McLafferty, T. P. Begley^*

^*Corresponding author for this work

Molecular Biosciences

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138 Scopus citations

Abstract

ThiFSGH and ThiI are required for the biosynthesis of the thiazole moiety of thiamin in Escherichia coli. The overproduction, purification, and characterization of ThiFS and the identification of two of the early steps in the biosynthesis of the thiazole moiety of thiamin are described here. ThiS isolated from E. coli thiI⁺ is posttranslationally modified by converting the carboxylic acid group of the thiocarboxylate because ThiS isolated from a thiI^- strain does not contain this modification. ThiF catalyzes the adenylation by ATP of the carboxyl-terminal glycine of ThiS. This reaction is likely to be involved in the activation of ThiS for sulfur transfer from cysteine or from a cysteine-derived sulfur donor.

Original language	English (US)
Pages (from-to)	16555-16560
Number of pages	6
Journal	Journal of Biological Chemistry
Volume	273
Issue number	26
DOIs	https://doi.org/10.1074/jbc.273.26.16555
State	Published - Jun 26 1998

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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Taylor, S. V., Kelleher, N. L., Kinsland, C., Chiu, H. J., Costello, C. A., Backstrom, A. D., McLafferty, F. W., & Begley, T. P. (1998). Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation. Journal of Biological Chemistry, 273(26), 16555-16560. https://doi.org/10.1074/jbc.273.26.16555

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title = "Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation",

abstract = "ThiFSGH and ThiI are required for the biosynthesis of the thiazole moiety of thiamin in Escherichia coli. The overproduction, purification, and characterization of ThiFS and the identification of two of the early steps in the biosynthesis of the thiazole moiety of thiamin are described here. ThiS isolated from E. coli thiI+ is posttranslationally modified by converting the carboxylic acid group of the thiocarboxylate because ThiS isolated from a thiI- strain does not contain this modification. ThiF catalyzes the adenylation by ATP of the carboxyl-terminal glycine of ThiS. This reaction is likely to be involved in the activation of ThiS for sulfur transfer from cysteine or from a cysteine-derived sulfur donor.",

author = "Taylor, {S. V.} and Kelleher, {N. L.} and C. Kinsland and Chiu, {H. J.} and Costello, {C. A.} and Backstrom, {A. D.} and McLafferty, {F. W.} and Begley, {T. P.}",

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doi = "10.1074/jbc.273.26.16555",

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T1 - Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation

AU - Taylor, S. V.

AU - Kelleher, N. L.

AU - Kinsland, C.

AU - Chiu, H. J.

AU - Costello, C. A.

AU - Backstrom, A. D.

AU - McLafferty, F. W.

AU - Begley, T. P.

PY - 1998/6/26

Y1 - 1998/6/26

N2 - ThiFSGH and ThiI are required for the biosynthesis of the thiazole moiety of thiamin in Escherichia coli. The overproduction, purification, and characterization of ThiFS and the identification of two of the early steps in the biosynthesis of the thiazole moiety of thiamin are described here. ThiS isolated from E. coli thiI+ is posttranslationally modified by converting the carboxylic acid group of the thiocarboxylate because ThiS isolated from a thiI- strain does not contain this modification. ThiF catalyzes the adenylation by ATP of the carboxyl-terminal glycine of ThiS. This reaction is likely to be involved in the activation of ThiS for sulfur transfer from cysteine or from a cysteine-derived sulfur donor.

AB - ThiFSGH and ThiI are required for the biosynthesis of the thiazole moiety of thiamin in Escherichia coli. The overproduction, purification, and characterization of ThiFS and the identification of two of the early steps in the biosynthesis of the thiazole moiety of thiamin are described here. ThiS isolated from E. coli thiI+ is posttranslationally modified by converting the carboxylic acid group of the thiocarboxylate because ThiS isolated from a thiI- strain does not contain this modification. ThiF catalyzes the adenylation by ATP of the carboxyl-terminal glycine of ThiS. This reaction is likely to be involved in the activation of ThiS for sulfur transfer from cysteine or from a cysteine-derived sulfur donor.

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Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation

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