Cyanuric acid as nitrogen source for micro-organisms

1969 ◽  
Vol 67 (1) ◽  
pp. 1-5 ◽  
Author(s):  
H. L. Jensen ◽  
A. S. Abdel-Ghaffar
Keyword(s):  
Nitrogen Source ◽  
Cyanuric Acid ◽  
Micro Organisms

Evaluation of peptones from chicken waste as a nitrogen source for micro‐organisms

2020 ◽  
Author(s):  
A. Nakamura ◽  
H. Takahashi ◽  
S. Sulaiman ◽  
C. Phraephaisarn ◽  
S. Keeratipibul ◽  
...  
Keyword(s):  
Nitrogen Source ◽  
Chicken Waste ◽  
Micro Organisms

scholarly journals Molecular Basis of a Bacterial Consortium: Interspecies Catabolism of Atrazine

1998 ◽  
Vol 64 (1) ◽  
pp. 178-184 ◽  
Author(s):  
Mervyn L. de Souza ◽  
David Newcombe ◽  
Sam Alvey ◽  
David E. Crowley ◽  
Anthony Hay ◽  
...  
Keyword(s):  
Nitrogen Source ◽  
Southern Hybridization ◽  
Cyanuric Acid ◽  
Bacterial Species ◽  
Bacterial Consortium ◽  
Triazine Ring ◽  
Carbon And Nitrogen ◽  
Consortium Member ◽  
Ring Compounds ◽  
Pure Cultures

ABSTRACT Pseudomonas sp. strain ADP contains the genes,atzA, -B, and -C, that encode three enzymes which metabolize atrazine to cyanuric acid. Atrazine-catabolizing pure cultures isolated from around the world contain genes homologous to atzA, -B, and -C. The present study was conducted to determine whether the same genes are present in an atrazine-catabolizing bacterial consortium and how the genes and metabolism are subdivided among member species. The consortium contained four or more bacterial species, but two members, Clavibacter michiganese ATZ1 andPseudomonas sp. strain CN1, collectively mineralized atrazine. C. michiganese ATZ1 released chloride from atrazine, produced hydroxyatrazine, and contained a homolog to theatzA gene that encoded atrazine chlorohydrolase. C. michiganese ATZ1 stoichiometrically metabolized hydroxyatrazine to N-ethylammelide and contained genes homologous toatzB and atzC, suggesting that either a functional AtzB or -C catalyzed N-isopropylamine release from hydroxyatrazine. C. michiganese ATZ1 grew on isopropylamine as its sole carbon and nitrogen source, explaining the ability of the consortium to use atrazine as the sole carbon and nitrogen source. A second consortium member, Pseudomonassp. strain CN1, metabolized the N-ethylammelide produced byC. michiganese ATZ1 to transiently form cyanuric acid, a reaction catalyzed by AtzC. A gene homologous to the atzCgene of Pseudomonas sp. strain ADP was present, as demonstrated by Southern hybridization and PCR. Pseudomonassp. strain CN1, but not C. michiganese, metabolized cyanuric acid. The consortium metabolized atrazine faster than didC. michiganese individually. Additionally, the consortium metabolized a much broader set of triazine ring compounds than did previously described pure cultures in which the atzABCgenes had been identified. These data begin to elucidate the genetic and metabolic bases of catabolism by multimember consortia.

Isolation of a Bacterial Community Able to Use Cyanuric Acid as Its Sole Carbon and Nitrogen Source

2010 ◽  
Vol 150 ◽  
pp. 564-564
Author(s):  
I.A. Silva-Lemus ◽  
C.E. Vásquez-Ortiz ◽  
D. Ahuatzi-Chacón ◽  
A.M. Salmerón-Alcocer ◽  
N. Ruiz-Ordaz ◽  
...  
Keyword(s):  
Bacterial Community ◽  
Nitrogen Source ◽  
Cyanuric Acid ◽  
Carbon And Nitrogen

Mineralization of melamine and cyanuric acid as sole nitrogen source by newly isolated Arthrobacter spp. using a soil-charcoal perfusion method

2015 ◽  
Vol 31 (5) ◽  
pp. 785-793 ◽  
Author(s):  
Takashi Hatakeyama ◽  
Kazuhiro Takagi ◽  
Kenichi Yamazaki ◽  
Futa Sakakibara ◽  
Koji Ito ◽  
...  
Keyword(s):  
Nitrogen Source ◽  
Cyanuric Acid ◽  
Sole Nitrogen Source ◽  
Soil Charcoal ◽  
Perfusion Method

scholarly journals On the Origins of Cyanuric Acid Hydrolase: Purification, Substrates, and Prevalence of AtzD from Pseudomonas sp. Strain ADP

2003 ◽  
Vol 69 (6) ◽  
pp. 3653-3657 ◽  
Author(s):  
Isaac Fruchey ◽  
Nir Shapir ◽  
Michael J. Sadowsky ◽  
Lawrence P. Wackett
Keyword(s):  
Nitrogen Source ◽  
Cyanuric Acid ◽  
Sole Nitrogen Source ◽  
Pseudomonas Sp ◽  
Acid Hydrolase

ABSTRACT Cyanuric acid hydrolase (AtzD) from Pseudomonas sp. strain ADP was purified to homogeneity. Of 22 cyclic amides and triazine compounds tested, only cyanuric acid and N-methylisocyanuric acid were substrates. Other cyclic amidases were found not to hydrolyze cyanuric acid. Ten bacteria that use cyanuric acid as a sole nitrogen source for growth were found to contain either atzD or trzD, but not both genes.

Review of the Radiation Damage Problem of Organic Specimens in Electron Microscopy

1973 ◽  
Vol 31 ◽  
pp. 476-477
Author(s):  
L. Reimer
Keyword(s):  
Electron Microscopy ◽  
Radiation Damage ◽  
Irradiation Time ◽  
Dose Effect ◽  
Primary Process ◽  
Thin Specimen ◽  
Secondary Damage ◽  
Small Doses ◽  
Micro Organisms ◽  
Damage Processes

Most information about a specimen is obtained by elastic scattering of electrons, but one cannot avoid inelastic scattering and therefore radiation damage by ionisation as a primary process of damage. This damage is a dose effect, being proportional to the product of lectron current density j and the irradiation time t in Coul.cm−2 as long as there is a negligible heating of the specimen.Therefore one has to determine the dose needed to produce secondary damage processes, which can be measured quantitatively by a chemical or physical effect in the thin specimen. The survival of micro-organisms or the decrease of photoconductivity and cathodoluminescence are such effects needing very small doses (see table).

Functional amyloid: widespread in Nature, diverse in purpose

2014 ◽  
Vol 56 ◽  
pp. 207-219 ◽  
Author(s):  
Chi L.L. Pham ◽  
Ann H. Kwan ◽  
Margaret Sunde
Keyword(s):  
Spider Silk ◽  
Epigenetic Inheritance ◽  
Fibrillar Structure ◽  
Cytoplasmic Polyadenylation ◽  
Functional Amyloid ◽  
Interacting Protein ◽  
Diverse Range ◽  
Element Binding Protein ◽  
Functional Amyloids ◽  
Micro Organisms

Amyloids are insoluble fibrillar protein deposits with an underlying cross-β structure initially discovered in the context of human diseases. However, it is now clear that the same fibrillar structure is used by many organisms, from bacteria to humans, in order to achieve a diverse range of biological functions. These functions include structure and protection (e.g. curli and chorion proteins, and insect and spider silk proteins), aiding interface transitions and cell–cell recognition (e.g. chaplins, rodlins and hydrophobins), protein control and storage (e.g. Microcin E492, modulins and PMEL), and epigenetic inheritance and memory [e.g. Sup35, Ure2p, HET-s and CPEB (cytoplasmic polyadenylation element-binding protein)]. As more examples of functional amyloid come to light, the list of roles associated with functional amyloids has continued to expand. More recently, amyloids have also been implicated in signal transduction [e.g. RIP1/RIP3 (receptor-interacting protein)] and perhaps in host defence [e.g. aDrs (anionic dermaseptin) peptide]. The present chapter discusses in detail functional amyloids that are used in Nature by micro-organisms, non-mammalian animals and mammals, including the biological roles that they play, their molecular composition and how they assemble, as well as the coping strategies that organisms have evolved to avoid the potential toxicity of functional amyloid.

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