Biosynthesis of Streptococcal Cell Walls:
            <i>N</i>
            -Acetyl-
            <scp>d</scp>
            -Muramic Acid

Barkulis, S. S.; Boltralik, J. J.; Hankin, Hilda; Heymann, H

doi:10.1128/jb.94.4.963-965.1967

Cited by 3 publications

(2 citation statements)

References 14 publications

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“…The above results suggested that the temperature-dependent variation in the synthesis of the A-486-Var groupspecific carbohydrate could be related to a difference in the rate of an enzyme-mediated incorporation of N-acetylglucosamine into the cell wall. The presence of such an enzyme, UDP-Nacetylglucosamine transferase, had been suggested in previous reports (2,13,16). Studies were therefore carried out to confinn this hypothesis with the enzyme system associated with protoplast membranes as described by Markovitz and Dorfman (13) and by Zeleznick et al (20).…”

Section: 3mentioning

confidence: 87%

Temperature-dependent variation in the synthesis of streptococcal group-specific carbohydrate. II. Biosynthetic studies in group A and variant strains

Ayoub¹

1978

J Bacteriol

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The biosynthesis of the cell wall polysaccharide and peptidoglycan of group A and A-486-Var streptococci was studied with N-acetyl-[14C]glucosamine, UDP-N-acetyl-[14C]glucosamine, and [14C]glucose. The incorporation of N-acetyl-[14C]-glucosamine into the cell wall four times greater in the A-486-Var cells than in the group A cells. However, the percentage of the total label incorporated into the cell wall polysaccharide at 37 degrees C by the A-486-Var strain was 12%, compared with 66% for the group A cells. When the A-486-Var was grown at 22 degrees C, the proportion of the label incorporated into the cell wall polysaccharide increased to 41%. At 37 degrees C, N-acetyl-[14C]glucosamine was incorporated preferentially into the peptidoglycan of the A-486-Var; almost three times as much of the label was incorporated into the peptidoglycan at 37 degrees C as was incorporated at 22 degrees C. Studies with protoplast membranes of these organisms showed similar differences, with a fourfold greater uptake of UDP-N-acetyl-[14C]glucosamine by the A-486-Var membranes at both incubation temperatures. These studies suggest that a defect in the incorporation of N-acetylglucosamine into the side chain of the polysaccharide is present in the A-486-Var strain at a step following the synthesis of UDP-N-acetylglucosamine. This defect, which may involve the UDP-N-acetylglucosamine transferase, is temperature dependent in the A-486-Var strain.

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Section: 3mentioning

confidence: 87%

Temperature-dependent variation in the synthesis of streptococcal group-specific carbohydrate. II. Biosynthetic studies in group A and variant strains

Ayoub¹

1978

J Bacteriol

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“…(1960,1962). Optimal conditions for 14C incorporation were established for the purpose of using the alanineadding reaction as a sensitive analytical tool for the detection of biosynthetic UDPMurNAc from UDP-GlcNAc in cell homogenates of S. pyogenes in pursuit of our interest in muramic acid biosynthesis (Barkulis et al, 1967). We were able to isolate a small amount of the enzymatic product free from residual UDP-MurNAc and showed that it contained [14C]alanine and phosphorus in a ratio close to 1:2.…”

Section: °_mentioning

confidence: 99%

A synthesis of uridine(diphosphate)diphospho-N-acetylmuramic acid and its sue as an acceptor of L-alamine-14C

Heymann¹,

Turdiu²,

Lee³

et al. 1968

Biochemistry

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Amino Sugar Assimilation byEscherichia coli

Rolls

Shuster

1972

J Bacteriol

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The carbon skeleton of glucose is extensively randomized during conversion to cell wall glucosamine by Escherichia coli K-12. Exogenous glucosamine- 1 - 14 C is selectively oxidized, and isotope incorporation into cellular glucosamine is greatly diluted during assimilation. A mutant unable to grow with N -acetylglucosamine as a carbon and energy source was isolated from E. coli K-12. This mutant was found to be defective in glucosamine-6-phosphate deaminase. Glucosamine- 1 - 14 C and N -acetylglucosamine- 1 - 14 C were assimilated during the growth of mutant cultures without degradation or carbon randomization. Assimilated isotopic carbon resided entirely in cell wall glucosamine and muramic acid. Some isotope dilution occurred from biosynthesis, but at high concentrations (0.2 m m ) of added N -acetylglucosamine nearly all cellular amino sugar was derived from the exogenous source. Growth of the mutant was inhibited with 1 m m N -acetylglucosamine.

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Biosynthesis of Streptococcal Cell Walls: N -Acetyl- d -Muramic Acid

Cited by 3 publications

References 14 publications

Temperature-dependent variation in the synthesis of streptococcal group-specific carbohydrate. II. Biosynthetic studies in group A and variant strains

Temperature-dependent variation in the synthesis of streptococcal group-specific carbohydrate. II. Biosynthetic studies in group A and variant strains

A synthesis of uridine(diphosphate)diphospho-N-acetylmuramic acid and its sue as an acceptor of L-alamine-14C

Amino Sugar Assimilation byEscherichia coli

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