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 ◽  
...  

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.

2002 ◽  
Vol 68 (12) ◽  
pp. 5973-5980 ◽  
Author(s):  
Lisa C. Strong ◽  
Charlotte Rosendahl ◽  
Gilbert Johnson ◽  
Michael J. Sadowsky ◽  
Lawrence P. Wackett

ABSTRACT Arthrobacter aurescens strain TC1 was isolated without enrichment by plating atrazine-contaminated soil directly onto atrazine-clearing plates. A. aurescens TC1 grew in liquid medium with atrazine as the sole source of nitrogen, carbon, and energy, consuming up to 3,000 mg of atrazine per liter. A. aurescens TC1 is metabolically diverse and grew on a wider range of s-triazine compounds than any bacterium previously characterized. The 23 s-triazine substrates serving as the sole nitrogen source included the herbicides ametryn, atratone, cyanazine, prometryn, and simazine. Moreover, atrazine substrate analogs containing fluorine, mercaptan, and cyano groups in place of the chlorine substituent were also growth substrates. Analogs containing hydrogen, azido, and amino functionalities in place of chlorine were not growth substrates. A. aurescens TC1 also metabolized compounds containing chlorine plus N-ethyl, N-propyl, N-butyl, N-s-butyl, N-isobutyl, or N-t-butyl substituents on the s-triazine ring. Atrazine was metabolized to alkylamines and cyanuric acid, the latter accumulating stoichiometrically. Ethylamine and isopropylamine each served as the source of carbon and nitrogen for growth. PCR experiments identified genes with high sequence identity to atzB and atzC, but not to atzA, from Pseudomonas sp. strain ADP.


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 ◽  
...  

2001 ◽  
Vol 67 (6) ◽  
pp. 2622-2626 ◽  
Author(s):  
Samantha J. Marshall ◽  
Graham F. White

ABSTRACT Four axenic bacterial species capable of biodegrading nitroglycerin (glycerol trinitrate [GTN]) were isolated from soil samples taken from a washwater soakaway at a disused GTN manufacturing plant. The isolates were identified by 16S rRNA gene sequence homology asPseudomonas putida, an Arthrobacter species, aKlebsiella species, and a Rhodococcus species. Each of the isolates utilized GTN as its sole nitrogen source and removed nitro groups sequentially from GTN to produce glycerol dinitrates and mononitrates (GMN), with the exception of theArthrobacter strain, which achieved removal of only the first nitro group within the time course of the experiment. TheKlebsiella strain exhibited a distinct preference for removal of the central nitro group from GTN, while the other five strains exhibited no such regioselectivity. All strains which removed a second nitro group from glycerol 1,2-dinitrate showed regiospecific removal of the end nitro group, thereby producing glycerol 2-mononitrate. Most significant was the finding that theRhodococcus species was capable of removing the final nitro group from GMN and thus achieved complete biodegradation of GTN. Such complete denitration of GTN has previously been shown only in mixed bacterial populations and in cultures of Penicillium corylophilum Dierckx supplemented with an additional carbon and nitrogen source. Hence, to the best of our knowledge, this is the first report of a microorganism that can achieve complete denitration of GTN.


2019 ◽  
Author(s):  
Chetan Kumar Arya ◽  
Swati Yadav ◽  
Jonathan Fine ◽  
Ana Casanal ◽  
Gaurav Chopra ◽  
...  

AbstractDimethylformamidase (DMFase) breaks down the human-made synthetic solvent N,N-dimethyl formamide(DMF) used extensively in industry(1). DMF is not known to exist in nature and was first synthesized in 1893. In spite of the recent origin of DMF, certain bacterial species such as Paracoccus, Pseudomonas, and Alcaligenes have evolved pathways to breakdown DMF and use them as carbon and nitrogen source for growth(2, 3). The work presented here provides a molecular basis for the ability of DMFase from Paracoccus to function in exacting conditions of high solvent concentrations, temperature and ionic strength to catalyze the hydrolysis of a stable amide bond. The structure reveals a multimeric complex of the α2β2 type or (α2β2)2 type. One of the three domains of the large subunit and the small subunit are hitherto undescribed folds and as yet of unknown evolutionary origin. The active site is made of a distinctive mononuclear iron that is coordinated by two tyrosine residues and a glutamic acid residue. The hydrolytic cleavage of the amide bond is catalyzed at the Fe3+ site with a proximal glutamate probably acting as the base. The change in the quaternary structure is salt dependent with high salt resulting in the larger oligomeric state. Kinetic characterization reveals an enzyme that shows cooperativity between subunits and the structure provides clues on the interconnection between the active sites.Significance StatementN,N-dimethyl formamide(DMF) is a commonly used industrial solvent that was first synthesized in 1893. The properties that make DMF a highly desired solvent also makes it a difficult compound to breakdown. Yet, certain bacteria have evolved to survive in environments polluted by DMF and have enzymes that breakdown DMF and use it as their carbon and nitrogen source. The molecular structure of the enzyme that breaks down the stable amide bond in these bacteria, reveals two new protein folds and a unique mononuclear iron active site. The work reported here provides the structural and biochemical framework to query the evolutionary origins of the protein, as well as in engineering this enzyme for use in bioremediation of a human made toxic solvent.


2021 ◽  
Author(s):  
Jin-Tian Ma ◽  
Li-Sheng Wang ◽  
Zhi Chai ◽  
Xin-Feng Chen ◽  
Bo-Cheng Tang ◽  
...  

Quinazoline skeletons are synthesized by amino acids catabolism/reconstruction combined with dimethyl sulfoxide insertion/cyclization for the first time. The amino acid acts as a carbon and nitrogen source through HI-mediated catabolism...


2012 ◽  
Vol 39 (8) ◽  
pp. 1169-1177 ◽  
Author(s):  
C. Juárez-Ramírez ◽  
R. Velázquez-García ◽  
N. Ruiz-Ordaz ◽  
J. Galíndez-Mayer ◽  
O. Ramos Monroy

2016 ◽  
Vol 45 (41) ◽  
pp. 16519-16525 ◽  
Author(s):  
Jiao Xue ◽  
Runwei Wang ◽  
Zongtao Zhang ◽  
Shilun Qiu

C, N co-modified niobium pentoxide (Nb2O5) nanoneedles have been successfully synthesized via a facile hydrothermal method with Niobium Chloride (NbCl5) as a precursor and triethylamine as both the carbon and nitrogen source.


2011 ◽  
Vol 2011 ◽  
pp. 1-4 ◽  
Author(s):  
Shiyi Ou ◽  
Jing Zhang ◽  
Yong Wang ◽  
Ning Zhang

A mixture of wheat bran with maize bran as a carbon source and addition of (NH4)SO4 as nitrogen source was found to significantly increase production of feruloyl esterase (FAE) enzyme compared with wheat bran as a sole carbon and nitrogen source. The optimal conditions in conical flasks were carbon source (30 g) to water 1 : 1, maize bran to wheat bran 1 : 2, (NH4)SO4 1.2 g and MgSO4 70 mg. Under these conditions, FAE activity was 7.68 mU/g. The FAE activity on the mixed carbon sources showed, high activity against the plant cell walls contained in the cultures.


2009 ◽  
Vol 325 (1-2) ◽  
pp. 243-253 ◽  
Author(s):  
A. Montoya-González ◽  
O. E. González-Navarro ◽  
B. Govaerts ◽  
K. D. Sayre ◽  
I. Estrada ◽  
...  

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