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Originally published In Press as doi:10.1074/jbc.M109377200 on November 8, 2001

J. Biol. Chem., Vol. 277, Issue 4, 2886-2896, January 25, 2002
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Oxidative Decarboxylation of UDP-Glucuronic Acid in Extracts of Polymyxin-resistant Escherichia coli
ORIGIN OF LIPID A SPECIES MODIFIED WITH 4-AMINO-4-DEOXY-L-ARABINOSE*

Steven D. BreazealeDagger , Anthony A. RibeiroDagger §, and Christian R. H. RaetzDagger

From the Dagger  Department of Biochemistry and the § Duke NMR Spectroscopy Center and Department of Radiology, Duke University Medical Center, Durham, North Carolina 27710

Addition of the 4-amino-4-deoxy-L-arabinose (L-Ara4N) moiety to the phosphate groups of lipid A is implicated in bacterial resistance to polymyxin and cationic antimicrobial peptides of the innate immune system. The sequences of the products of the Salmonella typhimurium pmrE and pmrF loci, both of which are required for polymyxin resistance, recently led us to propose a pathway for L-Ara4N biosynthesis from UDP-glucuronic acid (Zhou, Z., Lin, S., Cotter, R. J., and Raetz, C. R. H. (1999) J. Biol. Chem. 274, 18503-18514). We now report that extracts of a polymyxin-resistant mutant of Escherichia coli catalyze the C-4" oxidation and C-6" decarboxylation of [alpha -32P]UDP-glucuronic acid, followed by transamination to generate [alpha -32P]UDP-L-Ara4N, when NAD and glutamate are added as co-substrates. In addition, the [alpha -32P]UDP-L-Ara4N is formylated when N-10-formyltetrahydrofolate is included. These activities are consistent with the proposed functions of two of the gene products (PmrI and PmrH) of the pmrF operon. PmrI (renamed ArnA) was overexpressed using a T7 construct, and shown by itself to catalyze the unprecedented oxidative decarboxylation of UDP-glucuronic acid to form uridine 5'-(beta -L-threo-pentapyranosyl-4"-ulose diphosphate). A 6-mg sample of the latter was purified, and its structure was validated by NMR studies as the hydrate of the 4" ketone. ArnA resembles UDP-galactose epimerase, dTDP-glucose-4,6-dehydratase, and UDP-xylose synthase in oxidizing the C-4" position of its substrate, but differs in that it releases the NADH product.

* This work was supported in part by National Institutes of Health Grant GM-51310 (to C. R. H. R.), The Duke NMR Center is partially supported by National Institutes of Health NCI Grant P30-CA-14236 (to A. A. R.), NMR instrumentation in the Duke NMR Center was supported by the National Science Foundation, the National Institutes of Health, the North Carolina Biotechnology Center, and Duke University.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AY057445.

To whom correspondence should be addressed. Tel.: 919-684-5326; Fax: 919-684-8885; E-mail: raetz@biochem.duke.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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