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J Bacteriol. 1990 September; 172(9): 5160-5164

research-article

Biosynthetic elongation of isolated teichuronic acid polymers via glucosyl- and N-acetylmannosaminuronosyltransferases from solubilized cytoplasmic membrane fragments of Micrococcus luteus.

K M Hildebrandt and J S Anderson

Department of Biochemistry, College of Biological Sciences, University of Minnesota, St. Paul 55108.

ABSTRACT

Cytoplasmic membrane fragments of Micrococcus luteus catalyze in vitro biosynthesis of teichuronic acid from uridine diphosphate D-glucose (UDP-glucose), uridine diphosphate N-acetyl-D-mannosaminuronic acid (UDP-ManNAcA), and uridine diphosphate N-acetyl-D-glucosamine. Membrane fragments solubilized with Thesit (dodecyl alcohol polyoxyethylene ether) can utilize UDP-glucose and UDP-ManNAcA to effect elongation of teichuronic acid isolated from native cell walls. When UDP-glucose is the only substrate supplied, the detergent-solubilized glucosyltransferase incorporates a single glucosyl residue onto each teichuronic acid acceptor. When both UDP-glucose and UDP-ManNAcA are supplied, the glucosyltransferase and the N-acetylmannosaminuronosyltransferase act cooperatively to elongate the teichuronic acid acceptor by multiple additions of the disaccharide repeat unit. As shown by polyacrylamide gel electrophoresis, low-molecular-weight fractions of teichuronic acid are converted to higher-molecular-weight polymers by the addition of as many as 17 disaccharide repeat units.

J Bacteriol. 1990 September; 172(9): 5160-5164




This article has been cited by other articles:

  • Deng, L., Anderson, J. S. (1997). Biosynthesis of Teichuronic Acid in the Bacterial Cell Wall. PURIFICATION AND CHARACTERIZATION OF THE GLUCOSYLTRANSFERASE OF MICROCOCCUS LUTEUS. J. Biol. Chem. 272: 479-485 [Abstract] [Full Text]  


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