Open AccessAntibacterial Activity of N -Pentylpantothenamide Is Due to Inhibition of Coenzyme A Synthesis
Author(s) -
Jacob Thomas,
John E. Cronan
Publication year - 2010
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.01473-09
Subject(s) - moiety , cofactor , coenzyme a , biochemistry , in vitro , in vivo , chemistry , protein biosynthesis , enzyme , cleave , stereochemistry , biology , reductase , microbiology and biotechnology
Growth inhibition by the pantothenate analog N-pentylpantothenamide (N5-Pan) has been attributed to the accumulation of acyl carrier protein carrying a prosthetic group modified by incorporation of N5-Pan. This was attributed to an inability of the AcpH acyl carrier protein phosphodiesterase to cleave the N5-Pan-modified prosthetic group from the protein moiety. We report that AcpH readily removes the N5-Pan-modified prosthetic group both in vivo and in vitro and show that N5-Pan blocks coenzyme A synthesis.
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