Literature DB >> 20677756

Reagent for the detection of protein thiocarboxylates in the bacterial proteome: lissamine rhodamine B sulfonyl azide.

Kalyanaraman Krishnamoorthy1, Tadhg P Begley.   

Abstract

Protein thiocarboxylates are involved in the biosynthesis of thiamin, molybdopterin, thioquinolobactin, and cysteine. Sequence analysis suggests that this post-translational modification is widely distributed in bacteria. Here we describe the development of lissamine rhodamine B sulfonyl azide as a sensitive click reagent for the detection of protein thiocarboxylates and describe the use of this reagent to detect PdtH, a putative protein thiocarboxylate involved in the biosynthesis of the pyridine dithiocarboxylic acid siderophore, in the Pseudomonas stutzeri proteome.

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Year:  2010        PMID: 20677756      PMCID: PMC2927480          DOI: 10.1021/ja1034107

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN: 0002-7863            Impact factor:   15.419


  17 in total

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5.  Identification of an extracellular agent [correction of catalyst] of carbon tetrachloride dehalogenation from Pseudomonas stutzeri strain KC as pyridine-2, 6-bis(thiocarboxylate)

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3.  Protein thiocarboxylate-dependent methionine biosynthesis in Wolinella succinogenes.

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4.  Fluorescent probes for tracking the transfer of iron-sulfur cluster and other metal cofactors in biosynthetic reaction pathways.

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5.  Functional elucidation of TfuA in peptide backbone thioamidation.

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