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Evolutionary trace analysis of the -D-phosphohexomutase superfamily

Department of Biochemistry, University of Missouri-Columbia, Columbia, Missouri 65211, USA

(RECEIVED April 10, 2004; FINAL REVISION May 5, 2004; ACCEPTED May 5, 2004)

The -D-phosphohexomutase superfamily is composed of four related enzymes that catalyze a reversible, intramolecular phosphoryl transfer on their sugar substrates. The enzymes in this superfamily play important and diverse roles in carbohydrate metabolism in organisms from bacteria to humans. Recent structural and mechanistic studies of one member of this superfamily, phosphomannomutase/phosphoglucomutase (PMM/ PGM) from Pseudomonas aeruginosa, have provided new insights into enzyme mechanism and substrate recognition. Here we use sequence–sequence and sequence–structure comparisons via evolutionary trace analysis to examine 71 members of the -D-phosphohexomutase superfamily. These analyses show that key residues in the active site, including many of those involved in substrate contacts in the P. aeruginosa PMM/PGM complexes, are conserved throughout the enzyme family. Several important regions show class-specific differences in sequence that appear to be correlated with differences in substrate specificity exhibited by subgroups of the family. In addition, we describe the translocation of a 20-residue segment containing the catalytic phosphoserine of phosphoacetylglucosamine mutase, which uniquely identifies members of this subgroup.

Keywords: phosphohexomutase; evolutionary trace; enzyme superfamily; carbohydrate metabolism

Abbreviations: PGM, phosphoglucomutase • PMM/PGM, phosphomannomutase/phosphoglucomutase • PNGM, phosphoglucosamine mutase • PAGM, phosphoacetylglucosamine mutase • ET, evolutionary trace

Reprint requests to: Lesa J. Beamer, Department of Biochemistry, 117 Schweitzer Hall, University of Missouri-Columbia, Columbia, MO 65211, USA; e-mail: beamerl{at}missouri.edu; fax: (573) 884-4812.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04801104.

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