[54] Formation of dTDP-l-rhamnose from dTDP-d-glucose

Glaser, Luis; Kornfeld, Stuart

doi:10.1016/0076-6879(66)08058-3

Cited by 12 publications

(9 citation statements)

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“…These include the formation of GDP-L-fucose (26), GDP-colitose (27), GDP-D rhamnose and GDP-6-deoxY-D-talose (28) from GDP-D-mannOsej dTDP-L rhamnose (29,30) and dTDP-4-amino-4,6-dideoxyhexose (31, 32) from dTDP-D-glucose; CDP-paratose and CDP-ascarylose (33)(34)(35) from CDP-D glucose; and UDP-L-rhamnose from UDP-D-glucose (36). Bacterial extracts catalyze the formation of dTDP-4-amino-4,6-dideoxyhexose by the following reaction (31,32):…”

Section: Sugar Nucleotidesmentioning

confidence: 99%

Carbohydrate Metabolism

Neufeld¹,

Ginsburg²

1965

Annu. Rev. Biochem.

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This review covers recent advances in some fields of current interest, with emphasis on biosynthesis and metabolic controls. Whole areas of research, including transport, transformations of sugars not linked to nuc1eotides, the hexose monophosphate shunt, and the degradation of saccharides other than glycogen have been regretfully omitted. SUGAR NUCLEOTIDESIsolation.-The list of sugar nucleotides isolated from natural sources continues to grow. GDP-D-mannuronic acid has been isolated from brown algae (1), CDP-paratose from Salmonella paratyphi A (2), ADP-mannose, ADP-galactose and ADP-N -acetylglucosamine from corn grain (3); and from Azotobacter vinelandii, strain 0, two unusual CDP-linked sugars (a 2-0-methyl-deoxyaldose and a carboxylic acid ester thereof) have been isolated (4). While GDP-D-mannuronic acid and CDP-paratose presumably are intermediates in the synthesis of alginic acid and lipopolysaccharide, respec tively, possible functions of the remaining sugar nucleotides are not so obvious.Phosphorylases.-An enzyme from wheat germ catalyzes the phosphoroly sis of ADP-D-glucose to form ADP and a-D-glucose 1-phosphate (5). Inor ganic phosphate is incorporated into the terminal position of ADP. The reaction, which has not been reversed, goes equally well with ADP-D mannose, more slowly with other ADP sugars, and not at all with some nucleotides including UPD-D-glucose, GDP-D-mannose, and NAD. Another example of this type of reaction is the phosphorolysis of GDP-D-mannose catalyzed by extracts of yeast (6). The significance of these pathways is unknown, but possibly they serve to prevent excessive accumulation of sugar nucleotides. Interestingly, adenosine 5'-phosphosulfate can also un dergo phosphorolysis (6a).Pyrophosphorylases.-dTDP-D-galactose pyrophosphorylase activity has been separated from UDP-D-galactose pyrophosphorylase activity in prepa rations from mung bean seedlings (7) and Streptococcus faecalis grown on D-gaiactose (8). CDP-n-glucose pyrophosphorylase (9) and dTDP-n-glucose 1 The survey of literature pertaining to this review was concluded in August 1964. 2 The following abbreviations will be used in the text: ADP, CDP, GDP, IDP, dTDP, and UDP (the diphosphates of adenosine, cytidine, guanosine, ino sine, de oxythymidine, and uridine, respectively); NAD (nicotinamide adenine dinucleotide); and NADH (its reduced form). 297Annu. Rev. Biochem. 1965.34:297-312. Downloaded from www.annualreviews.org Access provided by Michigan State University Library on 02/06/15. For personal use only.Quick links to online content Further ANNUAL REVIEWS

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Section: Sugar Nucleotidesmentioning

confidence: 99%

Carbohydrate Metabolism

Neufeld¹,

Ginsburg²

1965

Annu. Rev. Biochem.

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“…dTDP-D-glucose 4,6-dehydratase (EC 4.2.1 .46) was measured in similar extracts except that the bacteria had been resuspended in 50 mM-Tris/HCl, 10 m~-MgCl,, 1 m-EDTA, pH 8. When incubated in 0.1 M-NaOH for 20 min, dTDP-4-keto-6-deoxy sugars develop a secondary absorption maximum at 318 nm (Okazaki et al, 1962) and the appearance of this absorption forms the kasis of the assay used (Glaser & Kornfeld, 1966). In the presence of dTDP-4-ketorhamnose 3,5-epirnerase (EC 5.1.3.13), the product of the dehydratase is converted to the rhamnose epimer which has the same absorption and hence would not be determined separately.…”

Section: E T H O D Smentioning

confidence: 99%

“…rhamnose was prepared enzymically from it in two stages by the methods of and Glaser & Kornfeld (1966). The overall yield was about 15 yo.…”

Section: E T H O D Smentioning

confidence: 99%

Biosynthesis of the Core Part of the Lipopolysaccharide of Pseudomonas aeruginosa

Asonganyi

Meadow

1980

Microbiology

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The incorporation of rhamnose and glucose into the core part of the lipopolysaccharide (LPS) of Pseudomonas aeruginosa was studied using enzyme preparations from strain PAC1 R and LPS-defective mutants derived from it. Crude membrane preparations from the LPS-defective mutant PAC556 transferred rhamnose from dTDP-L-[14C]rhamnose to material insoluble in trichloroacetic acid. The preparations contained both transferase enzyme and acceptor, the former being destroyed by heating. Between 60 and 70% of the radioactive rhamnose transferred to the membranes was extractable by aqueous phenol and non-diffusible. The material extracted did not move in any of the chromatography solvents tested and contained rhamnose as the sole radioactive component. Soluble dTDP-L-rhamnose-LPS rhamnosyltransferase was obtained from the parent strain PAC 1 R by ammonium sulphate precipitation of a 105000 g supernatant fraction from broken bacteria. It was most active at pH 8 with 5 mM-MgC1, and required heat-treated membranes of PAC556 as acceptor. This mutant, whose LPS lacks both 0-antigenic side-chains and rhamnose in the core, was shown to lack either the epimerase or the NADP-dependent oxidoreductase used to synthesize dTDPrhamnose. After preincubation with soluble transferase and UDPglucose, heated membranes of mutant strains PAC6 I 1, PAC6 12 and PAC605 could also act as acceptors for rhamnose. These mutants all lacked some or all of the glucose as well as the rhamnose from the core of their LPS and the experiments thus provided confirmation that rhamnose was the terminal hexose of the core in P. aeruginosa PAC1.

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“…The formation of dTDP-L-rhamnose from dTDP-D-glucose was assayed by the method of Glaser & Kornfeld (1966), and GDPmannose pyrophosphorylase activity was estimated by the method of Munch-Petersen (1962). Sugar nucleotides were purchased from Sigma.…”

Section: Experiments With Chloramphenicol and Actinomycin D ( I ) E'mentioning

confidence: 99%

Extracellular Polysaccharide Biosynthesis by Pseudomonas NCIB 11264. Studies on Precursor-forming Enzymes and Factors Affecting Exopolysaccharide Production by Washed Suspensions

Williams

Wimpenny

1980

Microbiology

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An assay was developed to measure the rate of exopolysaccharide formation by washed non-proliferating suspensions of Pseudomonas NCIB 11264 grown under a range of controlled environmental conditions. The specific activities of certain of the enzymes involved in the formation of the sugar nucleotide precursors of polysaccharide biosynthesis were also measured in steady-state populations. The level of enzyme activity did not reflect either the amount of extracellular polysaccharide produced or the rate at which glucose was incorporated into exopolysaccharide, which was dependent on medium composition, environmental factors, and the rate and stage of growth of the organism. The specific activities were not affected by either cultural conditions or the separate addition of actinomycin D and chloramphenicol, indicating a constitutive biosynthetic system.

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[54] Formation of dTDP-l-rhamnose from dTDP-d-glucose

Cited by 12 publications

References 10 publications

Carbohydrate Metabolism

Carbohydrate Metabolism

Biosynthesis of the Core Part of the Lipopolysaccharide of Pseudomonas aeruginosa

Extracellular Polysaccharide Biosynthesis by Pseudomonas NCIB 11264. Studies on Precursor-forming Enzymes and Factors Affecting Exopolysaccharide Production by Washed Suspensions

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