The Structure and Synthesis of the Liver
            <i>L. casei</i>
            Factor

Angier, Robert B.; Boothe, James H.; Hutchings, B. L.; Mowat, John H.; Semb, Joseph; Stokstad, E. L. R.; Subbarow, Y.; Waller, Coy W.; Cosulich, Donna B.; Fahrenbach, Marvin J.; Hultquist, Martin E.; Kuh, Erwin; Northey, E. H.; Seeger, Doris R.; Sickels, J. P.; Smith, James M.

doi:10.1126/science.103.2683.667

Cited by 209 publications

(24 citation statements)

References 6 publications

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“…The discovery of the structure of folic acid (Angier et al 1946) and of the glutaniic acid peptides associated with p-aminobenzoic acid (Ratner, Blanchard & Green, 1946) indicated that glutaniic acid can form homoglutarnic peptides in the living cell. This property is shown in the case of the D-isomer by the horno-D-glutamic acid nature of the capsular polypeptide of B. anthracis (Hanby & Rydon, 1946).…”

Section: Nature Of Glutanaic Acid Rnetaboliswmentioning

confidence: 99%

The Assimilation of Amino-acids by Bacteria: 4. The Action of Triphenylmethane Dyes on Glutamic Acid Assimilation

Gale

Mitchell

1947

Journal of General Microbiology

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SUMMARY:The level of glutamic acid concentration measured inside the streptococcal cell during assimilation represents a balance between the rate a t which the amino-acid is withdrawn from the external medium and the rate a t which it is metabolized within the cell.Treatment of the cells, prior to or during assimilation, with dyes of the triphenylmethane series results in raising the level of free glutamic acid attained within the cell. Evidence is presented that the triphenylmethane dyes prevent the metabolism of glutamic acid within the cell. The activity of the triphenylmethane molecule as an antibacterial agent and in raising the level of glutamic acid assimilation is increased by alkyl substitution and can be correlated with the lipid solubility of the dye.Dyes of the triphenylmethane series have long been known as effective antibacterial agents. Kligler (1918) showed that the quinonoid structure of the dye molecule is important for antimicrobial activity and that the effectiveness of the dyes is increased by substitution of alkyl radicles in the amino-groups of triamino-and diamino-triphenylmethanes. He showed that bacteria differ widely in their sensitivity to these dyestuffs and that, in general, Gram-positive organisms are more sensitive than Gram-negative species. The dyes fell into the following order of increasing effectiveness : fuchsin (1 CH,), methyl violet ( 5 CH,), crystal violet (6 CH,), malachite green (4CH,), brilliant green (4C2H5).

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Section: Nature Of Glutanaic Acid Rnetaboliswmentioning

confidence: 99%

The Assimilation of Amino-acids by Bacteria: 4. The Action of Triphenylmethane Dyes on Glutamic Acid Assimilation

Gale

Mitchell

1947

Journal of General Microbiology

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“…The latter was shown to be a component of folate, an essential vitamin (1). Analysis of folate biosynthesis in several bacterial species (27,31), including Streptococcus pneumoniae (24), revealed the following pathway:…”

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confidence: 99%

Sulfonamide resistance in Streptococcus pneumoniae: DNA sequence of the gene encoding dihydropteroate synthase and characterization of the enzyme

López¹,

Espinosa²,

Greenberg³

et al. 1987

J Bacteriol

122

106

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A chromosomal gene of Streptococcus pneumoniae carrying a spontaneous mutation to sulfonamide resistance was identified. Comparison of its DNA sequence with the wild-type sequence showed that the mutation, sul-d, consisted of an insert of 6 base pairs, a repeat of an adjacent 6-base-pair segment. The gene encoded a 34-kilodalton polypeptide, SulA, which as a dimer or trimer constituted the enzyme dihydropteroate synthase. This was shown by enzyme activity measurements, expression in minicells of Bacillus subtilis, and the amino-terminal sequence of the polypeptide product. Subcloning of the gene in an Eschenichia coli expression vector allowed purification of the enzyme to 80% homogeneity in a single step and at high yield. Although a deleted plasmid, pLS83, produced the mutant dihydropteroate synthase, it did not confer sulfonamide resistance in vivo. It is suggested that the SulA polypeptide is also a component of an enzyme that acts in another step of folate biosynthesis and that this step is inhibited in vivo by either free or conjugated sulfonamides.

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“…The core of the folate coenzyme structures was established in 1946 (1), and no modifications of this original structure were found until 1980 when the first structurally modified folate, methanopterin, was characterized (25,26). Methanopterin was isolated and characterized because of its involvement as a C1 carrier in the reduction of CO2 to CH4 in methanogenic archaebacteria where it functions analogously to folate (21).…”

mentioning

confidence: 99%

Distribution of folates and modified folates in extremely thermophilic bacteria

White

1991

J Bacteriol

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Analyses were made of the structures and levels of folates and modified folates present in extremely thermophilic bacteria. These procedures involved the chemical analysis of products resulting from the oxidative cleavage of the 6-substituted, folatelike tetrahydropterins present in the cells. Air-oxidized cell extracts of extreme thermophiles from two members of the archaebacterial order Thermococcales, Thermococcus celer and Pyrococcusfuriosus, contained only 7-methylpterin, indicating that these cells contain a modified folate with a methylated pterin. Cell extracts also contained 6-acetyl-7-methyl-7,8-dihydropterin, another product derived from the oxidative cleavage of a dimethylated folate, demonstrating that both the C-7 and C-9 carbons of the pterin were methylated. Extracts, however, contained neither p-aminobenzoylpolyglutamates nor methaniline, the oxidative cleavage products of folates and methanopterin, respectively, indicating that they contain a previously undescribed C1 carrier(s). On the basis of the level of the 7-methylpterin isolated, the levels of modified folate were 2 to 10 times higher than those typically found in mesophilic bacteria and 10 to 100 times less than the levels of methanopterin found in the methanogenic bacteria. Oxidized cell extracts of Sulfolobus spp. of the archaebacterial order Sulfolobaks contained only pterin, and, like members of the order Thermococcales, they contained neither p-aminobenzoylpolyglutamates nor methaniline. Oxidized cell extracts of the extreme thermophiles Pyrobaculum sp. strain H10 and Pyrodictium occultum, from the archaebacterial orders Thermoproteales and Pyrodictiales, respectively, and Thermotoga maritima, from the eubacterial order Thermotogales, contained pterin and p-aminobenzoylpolyglutamates, indicating that these cells contained unmodified folates. The levels of p-aminobenzoylpolyglutamates in these archaebacterial cell extracts indicate that the folates were present in the cells at levels 4 to 10 times higher than generally found in those mesophilic eubacteria which do not use folates in energy metabolism. The levels and chain lengths of the of p-aminobenzoylpolyglutamates present in Thermotoga maritima were typical of those found in mesophilic eubacteria.Folic acid and its polyglutamyl derivatives represent one of the central coenzymes found in biological systems where folic acid functions as a C1 carrier. The core of the folate coenzyme structures was established in 1946 (1), and no modifications of this original structure were found until 1980 when the first structurally modified folate, methanopterin, was characterized (25,26). Methanopterin was isolated and characterized because of its involvement as a C1 carrier in the reduction of CO2 to CH4 in methanogenic archaebacteria where it functions analogously to folate (21). (The close similarity between the biosynthesis of folate and the biosynthesis of methanopterin further supports the close connection between these C1 carriers [27,29,30,33].) Subsequent work has indicated that thi...

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The Structure and Synthesis of the Liver L. casei Factor

Cited by 209 publications

References 6 publications

The Assimilation of Amino-acids by Bacteria: 4. The Action of Triphenylmethane Dyes on Glutamic Acid Assimilation

The Assimilation of Amino-acids by Bacteria: 4. The Action of Triphenylmethane Dyes on Glutamic Acid Assimilation

Sulfonamide resistance in Streptococcus pneumoniae: DNA sequence of the gene encoding dihydropteroate synthase and characterization of the enzyme

Distribution of folates and modified folates in extremely thermophilic bacteria

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