This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by de Azevedo Wäsch, S. I.
Right arrow Articles by Leisinger, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by de Azevedo Wäsch, S. I.
Right arrow Articles by Leisinger, T.
Agricola
Right arrow Articles by de Azevedo Wäsch, S. I.
Right arrow Articles by Leisinger, T.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, May 2002, p. 2368-2375, Vol. 68, No. 5
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.5.2368-2375.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Transformation of Isopropylamine to L-Alaninol by Pseudomonas sp. Strain KIE171 Involves N-Glutamylated Intermediates

Susana I. de Azevedo Wäsch,1 Jan R. van der Ploeg,1,{dagger} Tere Maire,1 Alice Lebreton,1 Andreas Kiener,2 and Thomas Leisinger1*

Institute of Microbiology, ETH Zentrum, LFV, CH-8092 Zürich,1 Lonza AG, CH-3930 Visp, Switzerland2

Received 12 November 2001/ Accepted 4 February 2002

Pseudomonas sp. strain KIE171 was able to grow with isopropylamine or L-alaninol [S-(+)-2-amino-1-propanol] as the sole carbon source, but not with D-alaninol. To investigate the hypothesis that L-alaninol is an intermediate in the degradation of isopropylamine, two mini-Tn5 mutants unable to utilize both isopropylamine and L-alaninol were isolated. Whereas mutant KIE171-BI transformed isopropylamine to L-alaninol, mutant KIE171-BII failed to do so. The two genes containing a transposon insertion were cloned, and the DNA regions flanking the insertions were sequenced. Two clusters, one comprising eight ipu (isopropylamine utilization) genes (ipuABCDEFGH) and the other encompassing two genes (ipuI and orf259), were identified. Comparisons of sequences of the deduced Ipu proteins and those in the database suggested that isopropylamine is transported into the cytoplasm by a putative permease, IpuG. The next step, the formation of {gamma}-glutamyl-isopropylamide from isopropylamine, ATP, and L-glutamate, was shown to be catalyzed by IpuC, a {gamma}-glutamylamide synthetase. {gamma}-Glutamyl-isopropylamide is then subjected to stereospecific monooxygenation by the hypothetical four-component system IpuABDE, thereby yielding {gamma}-glutamyl-L-alaninol [{gamma}(L-glutamyl)-L-hydroxy-isopropylamide]. Enzymatic hydrolysis by a hydrolase, IpuF, was shown to finally liberate L-alaninol and to regenerate L-glutamate. No gene(s) encoding an enzyme for the next step in the degradation of isopropylamine was found in the ipu clusters. Presumably, L-alaninol is oxidized by an alcohol dehydrogenase to yield L-2-aminopropionaldehyde or it is deaminated by an ammonia lyase to propionaldehyde. Genetic evidence indicated that the aldehyde formed is then further oxidized by the hypothetical aldehyde dehydrogenases IpuI and IpuH to either L-alanine or propionic acid, compounds which can be processed by reactions of the intermediary metabolism.

* Corresponding author. Mailing address: Institute of Microbiology, ETH Zentrum, LFV, CH-8092 Zürich, Switzerland. Phone: (41)-1-6323324. Fax: (41)-1-6321385. E-mail: leisinger{at}micro.biol.ethz.ch.

{dagger} Present address: Institute for Oral Microbiology and General Immunology, Center for Dental and Oral Medicine and Maxillofacial Surgery, University of Zürich, CH-8028 Zürich, Switzerland.

Applied and Environmental Microbiology, May 2002, p. 2368-2375, Vol. 68, No. 5
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.5.2368-2375.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Garcia-Hernandez, R., Moraleda-Munoz, A., Castaneda-Garcia, A., Perez, J., Munoz-Dorado, J. (2009). Myxococcus xanthus Pph2 Is a Manganese-dependent Protein Phosphatase Involved in Energy Metabolism. J. Biol. Chem. 284: 28720-28728 [Abstract] [Full Text]  
  • Shapir, N., Mongodin, E. F., Sadowsky, M. J., Daugherty, S. C., Nelson, K. E., Wackett, L. P. (2007). Evolution of Catabolic Pathways: Genomic Insights into Microbial s-Triazine Metabolism. J. Bacteriol. 189: 674-682 [Full Text]  
  • Kurihara, S., Oda, S., Kato, K., Kim, H. G., Koyanagi, T., Kumagai, H., Suzuki, H. (2005). A Novel Putrescine Utilization Pathway Involves {gamma}-Glutamylated Intermediates of Escherichia coli K-12. J. Biol. Chem. 280: 4602-4608 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»