ArticleProtein science : a publication of the Protein Society2001
A cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus is actually a broad specificity phosphatase.
Article in Protein science : a publication of the Protein Society, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 48 citations in OpenAlex.
- Characterization of an extremophile bacterial acid phosphatase derived from metagenomics analysis.Microbial biotechnology · 2024Article
- Assessment of the Effects of Triticonazole on Soil and Human Health.Molecules (Basel, Switzerland) · 2022Article
- Proposed carrier lipid-binding site of undecaprenyl pyrophosphate phosphatase from Escherichia coli.The Journal of biological chemistry · 2014Article
- Functional characterization of two members of histidine phosphatase superfamily in Mycobacterium tuberculosis.BMC microbiology · 2013Article
- Structural units important for activity of a novel-type phosphoserine phosphatase from Hydrogenobacter thermophilus TK-6 revealed by crystal structure analysis.The Journal of biological chemistry · 2013Article
- Crystallization and preliminary X-ray diffraction analysis of a novel type of phosphoserine phosphatase from Hydrogenobacter thermophilus TK-6.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Discovery and analysis of cofactor-dependent phosphoglycerate mutase homologs as novel phosphoserine phosphatases in Hydrogenobacter thermophilus.The Journal of biological chemistry · 2012Article
- Article
- Structure and activity of the metal-independent fructose-1,6-bisphosphatase YK23 from Saccharomyces cerevisiae.The Journal of biological chemistry · 2010Article
- Quantitative proteomics identification of phosphoglycerate mutase 1 as a novel therapeutic target in hepatocellular carcinoma.Molecular cancer · 2010Article
- Structural and biochemical studies of TIGAR (TP53-induced glycolysis and apoptosis regulator).The Journal of biological chemistry · 2009Article
- Identification of isopentenol biosynthetic genes from Bacillus subtilis by a screening method based on isoprenoid precursor toxicity.Applied and environmental microbiology · 2007Article
- Characterization of cofactor-dependent and cofactor-independent phosphoglycerate mutases from Archaea.Extremophiles : life under extreme conditions · 2007Article
- A phosphatase activity of Sts-1 contributes to the suppression of TCR signaling.Molecular cell · 2007Article
- Structure and molecular mechanism of Bacillus anthracis cofactor-independent phosphoglycerate mutase: a crucial enzyme for spores and growing cells of Bacillus species.Biophysical journal · 2007Article
- Structural and functional analysis of Rv3214 from Mycobacterium tuberculosis, a protein with conflicting functional annotations, leads to its characterization as a phosphatase.Journal of bacteriology · 2006Article
- Domain-based small molecule binding site annotation.BMC bioinformatics · 2006Article
- Hyaluronidases: their genomics, structures, and mechanisms of action.Chemical reviews · 2006Review
- Cloning, expression, purification and preliminary crystallographic data for Rv3214 (EntD), a predicted cofactor-dependent phosphoglycerate mutase from Mycobacterium tuberculosis.Acta crystallographica. Section F, Structural biology and crystallization communications · 2005Article
- Regulation of ecdysteroid signalling during Drosophila development: identification, characterization and modelling of ecdysone oxidase, an enzyme involved in control of ligand concentration.The Biochemical journal · 2005Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
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Abstract
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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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.