Mass spectral determination of phosphopantetheinylation specificity for carrier proteins in  Mycobacterium tuberculosis | Zendy

Jung James | Zendy; Bashiri Ghader | Zendy; Johnston Jodie M. | Zendy; Baker Edward N. | Zendy

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Mass spectral determination of phosphopantetheinylation specificity for carrier proteins in Mycobacterium tuberculosis

Author(s) -

Jung James,

Bashiri Ghader,

Johnston Jodie M.,

Baker Edward N.

Publication year - 2016

Publication title -

febs open bio

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.718

H-Index - 31

ISSN - 2211-5463

DOI - 10.1002/2211-5463.12140

Subject(s) - polyketide , mycobacterium tuberculosis , serine , biochemistry , acyl carrier protein , chemistry , identification (biology) , biology , mycobacterium , computational biology , bacteria , tandem mass spectrometry , biosynthesis , tuberculosis , mass spectrometry , enzyme , genetics , chromatography , medicine , pathology , botany

Phosphopantetheinyl transferases ( PPT ases) are key elements in the modular syntheses performed by multienzyme systems such as polyketide synthases. PPT ases transfer phosphopantetheine derivatives from Coenzyme A to carrier proteins ( CP s), thus orchestrating substrate supply. We describe an efficient mass spectrometry‐based protocol for determining CP specificity for a particular PPT ase in organisms possessing several candidate PPT ases. We show that the CP s MbtL and PpsC, both involved in synthesis of essential metabolites in Mycobacterium tuberculosis , are exclusively activated by the type 2 PPT ase PptT and not the type 1 AcpS. The assay also enables conclusive identification of the reactive serine on each CP .

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