Nutrition of Vitreoscilla stercoraria

1975 ◽  
Vol 21 (12) ◽  
pp. 1947-1951 ◽  
Author(s):  
D. C. Mayfield ◽  
A. S. Kester
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Defined Medium ◽  
Good Growth ◽  
Aspartate Family

The present study has shown that the glutamate or aspartate families, plus the aromatic amino acid family are required for growth of Vitreoscilla stercoraria. Furthermore, glutamine can substitute for the glutamate family, asparagine and methionine can replace the aspartate family, and tyrosine can substitute for the aromatic family. Amino acids which are easily oxidized by this organism, particularly serine and cysteine, stimulated growth. From these data, a defined medium was devised, which contained the fewest amino acids that could support good growth of V. stercoraria.

CHEMICALLY DEFINED MEDIUM FOR GROWTH OF MICROCOCCUS LYSODEIKTICUS

1961 ◽  
Vol 7 (1) ◽  
pp. 27-32 ◽  
Author(s):  
E. A. Grula ◽  
Shing-kei Luk ◽  
Yung-chieh Chu
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Defined Medium ◽  
Good Growth ◽  
Chemically Defined Medium ◽  
Free Base ◽  
Specific Amino Acid ◽  
Absolute Requirement ◽  
Adenylic Acid ◽  
Amino Acid Requirements

A chemically defined medium for growth of M. lysodeikticus is presented. The organism possesses a relatively nonspecific but absolute purine requirement that can best be satisfied by the free base hypoxanthine although adenine also allows some growth. A substitution for hypoxanthine, however, can be made by inosine, adenosine, or adenylic acid, but not by guanosine or guanylic acid. Although biotin stimulates growth, equally good growth occurs using biocytin or biotiu-d-sulphoxide. Less stimulation is apparent using desthiobiotin, dl-oxybiotin, or biotirt-l-sulphoxide. Although amino acids are necessary for growth, no absolute requirement for a specific amino acid can be demonstrated. The amino acid requirements need to be defined in terms of those amino acids which support good growth in the presence or absence of glutamic acid.

scholarly journals Human transferrin receptor internalization is partially dependent upon an aromatic amino acid on the cytoplasmic domain.

1990 ◽  
Vol 1 (4) ◽  
pp. 369-377 ◽  
Author(s):  
T E McGraw ◽  
F R Maxfield
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Rate Constant ◽  
Transferrin Receptor ◽  
Aromatic Amino Acid ◽  
Opposite Polarity ◽  
Receptor Internalization ◽  
Aromatic Side Chain ◽  
Human Transferrin ◽  
Human Transferrin Receptor

The objective of this work is to identify the elements of the human transferrin receptor that are involved in receptor internalization, intracellular sorting, and recycling. We have found that an aromatic side chain at position 20 on the cytoplasmic portion of the human transferrin receptor is required for efficient internalization. The wild-type human transferrin receptor has a tyrosine at this position. Replacement of the Tyr-20 with an aromatic amino acid does not alter the rate constant of internalization, whereas substitution with the nonaromatic amino acids serine, leucine, or cysteine reduces the internalization rate constant approximately three-fold. These results are consistent with similar studies of other receptor systems that have also documented the requirement for a tyrosine in rapid internalization. The amino terminus of the transferrin receptor is cytoplasmic, with the tyrosine 41 amino acids from the membrane. These two features distinguish the transferrin receptor from the other membrane proteins for which the role of tyrosine in internalization has been examined, because these proteins have the opposite polarity with respect to the membrane and because the tyrosines are located closer to the membrane (within 25 amino acids). The externalization rate for the recycling of the transferrin receptor is not altered by any of these substitutions, demonstrating that the aromatic amino acid internalization signal is not required for the efficient exocytosis of internalized receptor.

scholarly journals Amino acids and peptides. X. Leu-enkephalin analogues containing a fluorinated aromatic amino acid.

1989 ◽  
Vol 37 (3) ◽  
pp. 826-828 ◽  
Author(s):  
Mitsuko MAEDA ◽  
Koichi KAWASAKI ◽  
Joe WATANABE ◽  
Hiroshi KANETO
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Enkephalin Analogues

Amino acid uptake systems in Bacteroides ruminicola

1979 ◽  
Vol 25 (10) ◽  
pp. 1161-1168 ◽  
Author(s):  
Roselynn M. W. Stevenson
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nitrogen Sources ◽  
Amino Acid Uptake ◽  
Defined Medium ◽  
High Rate ◽  
Transport Systems ◽  
Acid Uptake ◽  
Chemical Structures ◽  
Kinetic Inhibition

Uptake of amino acids by Bacteroides ruminicola was observed in cells grown in a complete defined medium, containing ammonia as the nitrogen source. A high rate of uptake occurred only in fresh medium, as an inhibitory substance, possibly acetate, apparently accumulated during growth. All amino acids except proline were taken up and incorporated into cold trichloroacetic acid precipitable material. Different patterns of incorporation and different responses to 2,4-dinitrophenol and potassium ferricyanide indicated multiple uptake systems were involved. Kinetic inhibition patterns suggested six distinct systems were present for amino acid uptake, with specificities related to the chemical structures of the amino acids. Thus, the failure of free amino acids to act as sole nitrogen sources for growth of B. ruminicola is not due to the absence of transport systems for these compounds.

Selective Chemical Deuteration of Aromatic Amino Acids: A Retrospective

1997 ◽  
Author(s):  
K.S. Matthews ◽  
R. Matthews
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Protein Hydrolysate ◽  
Aromatic Amino Acids ◽  
Cellular Protein ◽  
Target Protein ◽  
Chemical Methods ◽  
Lactose Repressor ◽  
Selective Deuteration

In 1970 when we began post-doctoral work in the laboratory of Professor Oleg Jardetzky, selective deuteration of proteins to limit the number of protons present in the system for subsequent analysis was a newly developed and effective technique for NMR exploration of protein structure (Crespi et al., 1968; Markley et al., 1968). This approach allowed more facile assignment of specific resonances and generated the potential to follow the spectroscopic behavior of protons for a specific amino acid sidechain over a broad range of conditions. The primary method for labeling at that time involved growth of microorganisms (generally bacteria or algae) in D2O, followed by isolation of the deuteratedamino acids from a cellular protein hydrolysate. The amino acids isolated were, therefore, completely deuterated. Selective deuteration of a target protein was achieved by growing the producing organism on a mixture of completely deuterated and selected protonated amino acids under conditions that minimized metabolic interconversion of the amino acids. In one-dimensional spectra, aromatic amino acid resonances occur well downfield of the aliphatic resonances, and this region can therefore be examined somewhat independently by utilizing a single protonated aromatic amino acid to simplify the spectrum of the protein. However, the multiple spectral lines generated by aromatic amino acids can be complex and overlapping, precluding unequivocal interpretation. To address this complication, chemical methods were developed to both completely and selectively deuterate side chains of the aromatic amino acids, thereby avoiding the costly necessity of growing large volumes of microorganisms in D2O and subsequent tedious isolation procedures. In addition, selective deuteration of the amino acids simplified the resonance patterns and thereby facilitated assignment and interpretation of spectra. The methods employed were based on exchange phenomena reported in the literature and generated large quantities of material for use in growth of microorganisms for subsequent isolation of selectively labeled protein (Matthews et al., 1977a). The target protein for incorporation of the selectively deuterated aromatic amino acids generated by these chemical methods was the lactose repressor protein from Escherichia coli, and greatly simplified spectra of this 150,000 D protein were produced by this approach.

QUALITATIVE STUDIES OF SOIL MICROORGANISMS: IX. AMINO ACID REQUIREMENTS OF RHIZOSPHERE BACTERIA

1950 ◽  
Vol 28c (1) ◽  
pp. 1-6 ◽  
Author(s):  
R. H. Wallace ◽  
A. G. Lochhead
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Soil Microorganisms ◽  
Maximum Growth ◽  
Defined Medium ◽  
Chemically Defined Medium ◽  
Special Significance ◽  
Specific Amino Acid ◽  
Pronounced Decrease ◽  
Amino Acid Requirements

A study was made of the more specific amino acid requirements of bacteria from the rhizospheres of clover, flax, and wheat plants for which a chemically defined medium containing 23 amino acids provided essentials for maximum growth. Of seven groups of amino acids, the sulphur-containing group (cysteine, methionine, and taurine) was found to be of special significance, the omission of this group resulting in a pronounced decrease in the percentage of organisms able to develop. Further study of organisms dependent upon this group of amino acids for growth showed methionine to be by far the most essential compound. While evident for bacteria from the rhizosphere of all three crops, the effect was more pronounced in the case of clover than with flax or wheat.

scholarly journals Decoding the Complex Crossroad of Tryptophan Metabolic Pathways

2022 ◽  
Vol 23 (2) ◽  
pp. 787
Author(s):  
Giada Mondanelli ◽  
Claudia Volpi ◽  
Ciriana Orabona
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Metabolic Pathways ◽  
Aromatic Amino Acid ◽  
Living Cells ◽  
Cellular Homeostasis

Among the 20 amino acids needed for protein synthesis, Tryptophan (Trp) is an aromatic amino acid fundamental not only for the synthesis of the major components of living cells (namely, the proteins), but also for the maintenance of cellular homeostasis [...]

scholarly journals Histidine Degradation via an Aminotransferase Increases the Nutritional Flexibility of Candida glabrata

2014 ◽  
Vol 13 (6) ◽  
pp. 758-765 ◽  
Author(s):  
Sascha Brunke ◽  
Katja Seider ◽  
Martin Ernst Richter ◽  
Sibylle Bremer-Streck ◽  
Shruthi Ramachandra ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Candida Glabrata ◽  
Genomic Structure ◽  
Aromatic Amino Acids ◽  
Sole Source ◽  
Upstream Region ◽  
Content Type ◽  
Aromatic Amino Acid Aminotransferase

ABSTRACTThe ability to acquire nutrients during infections is an important attribute in microbial pathogenesis. Amino acids are a valuable source of nitrogen if they can be degraded by the infecting organism. In this work, we analyzed histidine utilization in the fungal pathogen of humansCandida glabrata. Hemiascomycete fungi, likeC. glabrataorSaccharomyces cerevisiae, possess no gene coding for a histidine ammonia-lyase, which catalyzes the first step of a major histidine degradation pathway in most other organisms. We show thatC. glabratainstead initializes histidine degradation via the aromatic amino acid aminotransferase Aro8. AlthoughARO8is also present inS. cerevisiaeand is induced by extracellular histidine, the yeast cannot use histidine as its sole nitrogen source, possibly due to growth inhibition by a downstream degradation product. Furthermore,C. glabratarelies only on Aro8 for phenylalanine and tryptophan utilization, sinceARO8, but not its homologueARO9, was transcriptionally activated in the presence of these amino acids. Accordingly, anARO9deletion had no effect on growth with aromatic amino acids. In contrast, inS. cerevisiae,ARO9is strongly induced by tryptophan and is known to support growth on aromatic amino acids. Differences in the genomic structure of theARO9gene betweenC. glabrataandS. cerevisiaeindicate a possible disruption in the regulatory upstream region. Thus, we show that, in contrast toS. cerevisiae,C. glabratahas adapted to use histidine as a sole source of nitrogen and that the aromatic amino acid aminotransferase Aro8, but not Aro9, is the enzyme required for this process.

scholarly journals The Growth Of Rhizobium in Synthetic Media

1961 ◽  
Vol 14 (3) ◽  
pp. 349 ◽  
Author(s):  
FJ Bergersen
Keyword(s):  
Amino Acids ◽  
Nitrogen Source ◽  
Exponential Growth ◽  
Defined Medium ◽  
Complete Medium ◽  
Good Growth ◽  
Chemically Defined Medium ◽  
Sodium Glutamate ◽  
Synthetic Media

A chemically defined medium for the growth of Rhizobium is described in which populations of up to 5 x 109 cells/ml were obtained. For the six strains of bacteria studied the complete medium supported exponential growth for two to five generations. The concentrations of biotin giving best growth varied ith strain between 125 and 250 f'g/l when the nitrogen source was sodium glutamate. NHt, NOs, and other amino acids, singly or in combination, did not upport as good growth as did sodium glutamate.

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