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Microbiology and Molecular Biology Reviews, March 2007, p. 36-47, Vol. 71, No. 1
1092-2172/07/$08.00+0     doi:10.1128/MMBR.00032-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Surprising Arginine Biosynthesis: a Reappraisal of the Enzymology and Evolution of the Pathway in Microorganisms

Ying Xu,1 Bernard Labedan,2* and Nicolas Glansdorff3

Marine Sciences Research Center, State University of New York at Stony Brook, Stony Brook, New York 11794-5000,1 Institut de Génétique et Microbiologie, CNRS UMR 8621, Université Paris Sud, Bâtiment 400, 91405 Orsay Cedex, France,2 Microbiology and Genetics, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussels, Belgium3

Summary: Major aspects of the pathway of de novo arginine biosynthesis via acetylated intermediates in microorganisms must be revised in light of recent enzymatic and genomic investigations. The enzyme N-acetylglutamate synthase (NAGS), which used to be considered responsible for the first committed step of the pathway, is present in a limited number of bacterial phyla only and is absent from Archaea. In many Bacteria, shorter proteins related to the Gcn5-related N-acetyltransferase family appear to acetylate L-glutamate; some are clearly similar to the C-terminal, acetyl-coenzyme A (CoA) binding domain of classical NAGS, while others are more distantly related. Short NAGSs can be single gene products, as in Mycobacterium spp. and Thermus spp., or fused to the enzyme catalyzing the last step of the pathway (argininosuccinase), as in members of the Alteromonas-Vibrio group. How these proteins bind glutamate remains to be determined. In some Bacteria, a bifunctional ornithine acetyltransferase (i.e., using both acetylornithine and acetyl-CoA as donors of the acetyl group) accounts for glutamate acetylation. In many Archaea, the enzyme responsible for glutamate acetylation remains elusive, but possible connections with a novel lysine biosynthetic pathway arose recently from genomic investigations. In some Proteobacteria (notably Xanthomonadaceae) and Bacteroidetes, the carbamoylation step of the pathway appears to involve N-acetylornithine or N-succinylornithine rather than ornithine. The product N-acetylcitrulline is deacetylated by an enzyme that is also involved in the provision of ornithine from acetylornithine; this is an important metabolic function, as ornithine itself can become essential as a source of other metabolites. This review insists on the biochemical and evolutionary implications of these findings.

* Corresponding author. Mailing address: Institut de Génétique et Microbiologie, CNRS UMR 8621, Université Paris Sud, Bâtiment 400, 91405 Orsay Cedex, France. Phone: 33 1 69 15 35 60. Fax: 33 1 69 15 72 96. E-mail: bernard.labedan{at}igmors.u-psud.fr.

Microbiology and Molecular Biology Reviews, March 2007, p. 36-47, Vol. 71, No. 1
1092-2172/07/$08.00+0     doi:10.1128/MMBR.00032-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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