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Title
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A cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus is actually a broad specificity phosphatase.
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Authors
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D.J.Rigden,
I.Bagyan,
E.Lamani,
P.Setlow,
M.J.Jedrzejas.
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Ref.
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Protein Sci, 2001,
10,
1835-1846.
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PubMed id
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Abstract
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The distribution of phosphoglycerate mutase (PGM) activity in bacteria is
complex, with some organisms possessing both a cofactor-dependent and a
cofactor-independent PGM and others having only one of these enzymes. Although
Bacillus species contain only a cofactor-independent PGM, genes homologous to
those encoding cofactor-dependent PGMs have been detected in this group of
bacteria, but in at least one case the encoded protein lacks significant PGM
activity. Here we apply sequence analysis, molecular modeling, and enzymatic
assays to the cofactor-dependent PGM homologs from B. stearothermophilus and B.
subtilis, and show that these enzymes are phosphatases with broad substrate
specificity. Homologs from other gram-positive bacteria are also likely to
possess phosphatase activity. These studies clearly show that the exploration of
genomic sequences through three-dimensional modeling is capable of producing
useful predictions regarding function. However, significant methodological
improvements will be needed before such analysis can be carried out
automatically.
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