An enzymatic release of antibiotic-containing peptidoglycan fragments from streptomycin-producing Streptomyces griseus

1980 ◽  
Vol 26 (2) ◽  
pp. 141-145 ◽  
Author(s):  
Gy. Barabás ◽  
I. Szabó ◽  
A. Ottenberger ◽  
V. Zs.-Nagy ◽  
G. Szabó
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Glutamic Acid ◽  
Streptomyces Griseus ◽  
Activity Analysis ◽  
Antibiotic Activity ◽  
Diaminopimelic Acid ◽  
Autolytic Enzyme ◽  
A Cell

A cell wall bound autolytic enzyme of a streptomycin-producing strain of Streptomyces griseus was investigated. The peptidoglycan fragments released by the enzyme showed antibiotic activity. Analysis of these fragments proved that streptomycin is bound to a cell wall peptide. The peptide contained the four amino acids characteristic of Streptomyces cell wall: alanine, glycine, diaminopimelic acid, and glutamine or glutamic acid.

scholarly journals Tracer studies on the biosynthesis of amino acids from lactate by Peptostreptococcus elsdenii

1967 ◽  
Vol 105 (1) ◽  
pp. 299-310 ◽  
Author(s):  
H. J. Somerville ◽  
J. L. Peel
Keyword(s):  
Amino Acids ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Tricarboxylic Acid Cycle ◽  
Carbon Chain ◽  
Tricarboxylic Acid ◽  
Diaminopimelic Acid ◽  
Reaction Sequence ◽  
Tracer Studies ◽  
Cell Fractions

Peptostreptococcus elsdenii, a strict anaerobe from the rumen, was grown on a medium containing yeast extract and [1−14C]- or [2−14C]-lactate. Radioisotope from lactate was found in all cell fractions, but mainly in the protein. The label in the protein fraction was largely confined to a few amino acids: alanine, serine, aspartic acid, glutamic acid and diaminopimelic acid. The alanine, serine, aspartic acid and glutamic acid were separated, purified and degraded to establish the distribution of 14C from lactate within the amino acid molecules. The labelling patterns in alanine and serine suggested their formation from lactate without cleavage of the carbon chain. The pattern in aspartic acid suggested formation by condensation of a C3 unit derived directly from lactate with a C1 unit, probably carbon dioxide. The distribution in glutamic acid was consistent with two possible pathways of formation: (a) by the reactions of the tricarboxylic acid cycle leading from oxaloacetate to 2-oxoglutarate, followed by transamination; (b) by a pathway involving the reaction sequence 2 acetyl-CoA→crotonyl-CoA→glutaconate→glutamate.

Nutritional requirements for cell wall synthesis in Micrococcus lysodeikticus

1969 ◽  
Vol 15 (4) ◽  
pp. 327-334
Author(s):  
M. P. Hatton
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Glutamic Acid ◽  
Dry Weight ◽  
Defined Medium ◽  
Complete Medium ◽  
Magnesium Ions ◽  
Cell Wall Synthesis ◽  
Micrococcus Lysodeikticus ◽  
Total Dry Weight

Preferential cell wall synthesis in Micrococcus lysodeikticus, as determined by an increase in the dry weight of the cell wall, took place in a medium containing DL-glutamic acid, DL-alanine, L-lysine, glycine, magnesium ions, glucose and phosphate buffer, pH 7.0. Cell wall synthesis could not be completely dissociated from protein synthesis in the 'cell wall' medium. The cell wall synthesized in the defined medium accounted for 40–56% of the total dry weight increase of the cells. Chloramphenicol had no effect on cell wall synthesis. Incorporation of uracil and guanine in the medium did not result in any increase in the amount of cell wall synthesized. DL-Glutamic acid alone, or a mixture of the three amino acids DL-alanine, L-lysine, and glycine, were capable of replacing the four amino acids present in the complete medium, but under these conditions the total dry weight of cell wall synthesized was only 75% of that produced in the complete medium. There was no reduction in cell wall synthesis when L-glutamic acid replaced DL-glutamic acid, L-alanine replaced DL-alanine, or sucrose replaced glucose in the cell wall medium. Deprivation of magnesium ions produced the greatest decrease in wall synthesis; this was the most important single factor involved in cell wall synthesis which was studied in the present investigation. There was no observable change in the chemical composition of the cell wall synthesized in the 'wall' medium when compared to that synthesized by cells grown in a complex medium.

scholarly journals The Amino Acids of the Cell Wall of Mycobacterium tuberculosis var. bovis, Strain BCG. Presence of a Poly(l-Glutamic Acid)

1973 ◽  
Vol 32 (3) ◽  
pp. 525-532 ◽  
Author(s):  
Juana Wietzerbin-Falszpan ◽  
Bhupesh C. Das ◽  
Claude Gros ◽  
Jean-Francois Petit ◽  
Edgar Lederer
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Mycobacterium Tuberculosis ◽  
Glutamic Acid

Incorporation of 14CO2 in amides and amino acids in rusted bean leaves

1975 ◽  
Vol 53 (12) ◽  
pp. 1244-1251 ◽  
Author(s):  
Vittorio Raggi
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Gradual Increase ◽  
Bean Leaves

Free amino acids were analyzed in healthy and rust-infected bean leaves incubated for 180–200 min in light, with 14CO2. In rusted leaves the radioactivity of the pool diminishes gradually to 42% in the flaking stage and the beginning of sporulation and then gradually increases in the following days to values of 197% after the secondary sporulation 11 days from infection. An increase in percentage of total labelling of aspartic acid, glutamic acid, and asparagine was noted, except just before sporulation, but above all, a marked and gradual increase in the labelling of glutamine was observed. This amide is probably assimilated to a greater degree by the fungus for the synthesis of its cell wall glucosamine. Diminution in the labelling of glycine and even more in the labelling of serine would instead be ascribed to the decrease in the photorespiratory activity.

scholarly journals Role of the Murein Precursor UDP-N-Acetylmuramyl-l-Ala-γ-d-Glu- meso-Diaminopimelic Acid-d-Ala-d-Ala in Repression of β-Lactamase Induction in Cell Division Mutants

2002 ◽  
Vol 184 (15) ◽  
pp. 4233-4239 ◽  
Author(s):  
Tsuyoshi Uehara ◽  
James T. Park
Keyword(s):  
Cell Wall ◽  
Cell Division ◽  
High Ratio ◽  
Diaminopimelic Acid ◽  
Breakdown Product ◽  
A Cell ◽  
Cell Wall Breakdown ◽  
Ts Mutant

ABSTRACT Certain β-lactam antibiotics induce the chromosomal ampC β-lactamase of many gram-negative bacteria. The natural inducer, though not yet unequivocally identified, is a cell wall breakdown product which enters the cell via the AmpG permease component of the murein recycling pathway. Surprisingly, it has been reported that β-lactamase is not induced by cefoxitin in the absence of FtsZ, which is required for cell division, or in the absence of penicillin-binding protein 2 (PBP2), which is required for cell elongation. Since these results remain unexplained, we examined an ftsZ mutant and other cell division mutants (ftsA, ftsQ, and ftsI) and a PBP2 mutant for induction of β-lactamase. In all mutants, β-lactamase was not induced by cefoxitin, which confirms the initial reports. The murein precursor, UDP-N-acetylmuramyl-l-Ala-γ-d-Glu-meso-diaminopimelic acid-d-Ala-d-Ala (UDP-MurNAc-pentapeptide), has been shown to serve as a corepressor with AmpR to repress β-lactamase expression in vitro. Our results suggest that β-lactamase is not induced because the fts mutants contain a greatly increased amount of corepressor which the inducer cannot displace. In the PBP2(Ts) mutant, in addition to accumulation of corepressor, cell wall turnover and recycling were greatly reduced so that little or no inducer was available. Hence, in both cases, a high ratio of repressor to inducer presumably prevents induction.

Specificity of cell wall labeling with tritiated diaminopimelic acid in Bacillus subtilis

1973 ◽  
Vol 19 (8) ◽  
pp. 1049-1051
Author(s):  
Siegfried Maier
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Glutamic Acid ◽  
Cell Walls ◽  
Diaminopimelic Acid ◽  
Chromatographic Purification ◽  
Membrane Chromatography

The suitability of tritiated 2,6-diaminopimelic acid (3H-DAP) as a label specific for cell walls was explored in Bacillus subtilis BC 102 grown in a medium enriched with 3H-DAP and an excess of L-lysine. Fractionation of labeled cells showed 57% of the activity in the cell wall and 28% in the membrane. Chromatography of labeled wall hydrolysates revealed two activity peaks: 62% in DAP and 29% in glutamic acid – alanine. Labeled membrane was devoid of activity in the DAP position. Chromatographic purification of the 3H-DAP improved specificity, giving 7% of the activity in the membrane and 85% in the wall. In such walls DAP accounted for 82% of the total wall activity. Therefore, only 69% of the total fixed purified 3H label remained with DAP in the wall.

Cell wall composition and incorporation of radio-labelled compounds by Veillonella alcalescens

1975 ◽  
Vol 21 (12) ◽  
pp. 2039-2047 ◽  
Author(s):  
P. F. Winter ◽  
E. A. Delwiche
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Nucleic Acid ◽  
Acid Synthesis ◽  
Cell Wall Composition ◽  
Diaminopimelic Acid ◽  
Nucleic Acid Synthesis ◽  
Gram Negative ◽  
Assay Methods ◽  
Pyruvate Level

The cell wall of Veillonella alcalescens was shown to have a typically Gram-negative appearance and composition. The wall contains 24% lipid, 0.8% phosphorus, and 6.8% hexosamine. It is estimated to contain about 5% murein, unlike the 24% reported by other for Veillonella parvula. The amounts of 19 amino acids, including diaminopimelic acid, were determined. Though Veillonella sp. cannot metabolize sugars for energy, V. alcalescens incorporates ribose and fructose by separate, specific mechanisms and uses most of the incorporated sugar in nucleic acid synthesis. Large excesses of either sugar in the medium do not repress gluconeogenesis from the pyruvate level. We have been unable to detect phosphoglyceromutase (EC 2.7.5.3) by several assay methods but have no indication of a gluconeogenic pathway other than reverse glycolysis.

scholarly journals Identification of amino acids and domains required for catalytic activity of DPPR synthase, a cell wall biosynthetic enzyme of Mycobacterium tuberculosis

Microbiology ◽  
2008 ◽  
Vol 154 (3) ◽  
pp. 736-743 ◽  
Author(s):  
Hairong Huang ◽  
Stefan Berg ◽  
John S. Spencer ◽  
Danny Vereecke ◽  
Wim D'Haeze ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Mycobacterium Tuberculosis ◽  
Catalytic Activity ◽  
Biosynthetic Enzyme ◽  
A Cell
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