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J Bacteriol. 1994 May; 176(9): 2525-2531

Lipid synthesis in mycobacteria: characterization of the biotin carboxyl carrier protein genes from Mycobacterium leprae and M. tuberculosis.

E Norman, K A De Smet, N G Stoker, C Ratledge, P R Wheeler and J W Dale

Molecular Microbiology Group, School of Biological Sciences, University of Surrey, Guildford, United Kingdom.

ABSTRACT

The causative agents of leprosy and tuberculosis, Mycobacterium leprae and Mycobacterium tuberculosis, have a lipid-rich cell envelope which contributes to virulence and antibiotic resistance. Acyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis, consists in mycobacteria of two subunits, one of which is biotinylated. Genes from M. leprae and M. tuberculosis encoding a biotinylated protein have been cloned and sequenced. Analysis of the derived protein sequences demonstrated the presence of biotin-binding sites and putative ATP-bicarbonate interactions sites, consistent with the proteins having a biotin carboxylase function as well as their being biotin carrier proteins.


J Bacteriol. 1994 May; 176(9): 2525-2531




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