Similar Regulation Patterns of Choline Monooxygenase, Phosphoethanolamine N-Methyltransferase and S-Adenosyl-l-Methionine Synthetase in Leaves of the Halophyte Atriplex nummularia L.

2005 ◽  
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Author(s):  
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Yusuke Kawaguchi ◽  
Tetsushi Azuma ◽  
Takashi Nanmori ◽  
Takeshi Yasuda
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Jailson Cavalcante Cunha ◽  
Maria Betânia Galvão dos Santos Freire ◽  
Hugo Alberto Ruiz ◽  
Jhonatha David Guimarães Silva

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Vol 190 (4) ◽  
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Jian-Kang Zhu ◽  
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PaulM. Hasegawa

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Vol 42 (3) ◽  
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Karen Cristina Fialho dos Santos ◽  
Marina Steffane Lopes da Silva ◽  
Luís Eduardo da Silva ◽  
Marcelo Alves Miranda ◽  
Maria Betânia Galvão dos Santos Freire
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2020 ◽  
Vol 153 ◽  
pp. 103574 ◽  
Author(s):  
Maria Camila de Barros Silva Leite ◽  
Maria Betânia Galvão dos Santos Freire ◽  
João Victor Jansen de Queiroz ◽  
Leonor Costa Maia ◽  
Gustavo Pereira Duda ◽  
...  

1998 ◽  
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Zheng Liang

Microbiology ◽  
2014 ◽  
Vol 160 (5) ◽  
pp. 929-940 ◽  
Author(s):  
Tomas Linder

Sixteen yeasts with sequenced genomes belonging to the ascomycete subphyla Saccharomycotina and Taphrinomycotina were assayed for their ability to utilize a variety of primary, secondary, tertiary and quartenary aliphatic amines as nitrogen sources. The results support a previously proposed pathway of quaternary amine catabolism whereby glycine betaine is first converted into choline, which is then cleaved to release trimethylamine, followed by stepwise demethylation of trimethylamine to release free ammonia. There were only a few instances of utilization of N-methylated glycine species (sarcosine and N,N-dimethylglycine), which suggests that this pathway is not intact in any of the species tested. The ability to utilize choline as a sole nitrogen source correlated strongly with the presence of a putative Rieske non-haem iron protein homologous to bacterial ring-hydroxylating oxygenases and plant choline monooxygenases. Deletion of the gene encoding the Rieske non-haem iron protein in the yeast Scheffersomyces stipitis abolished its ability to utilize choline as the sole nitrogen source, but did not affect its ability to use methylamine, dimethylamine, trimethylamine, ethylamine, diethylamine, ethanolamine or glycine as nitrogen sources. The gene was named CMO1 for putative choline monooxygenase 1. A bioinformatic survey of eukaryotic genomes showed that CMO1 homologues are found throughout the eukaryotic domain.


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