ArticleExtremophiles : life under extreme conditions2007
Characterization of cofactor-dependent and cofactor-independent phosphoglycerate mutases from Archaea.
Article in Extremophiles : life under extreme conditions, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- The return of metabolism: biochemistry and physiology of glycolysis.Biological reviews of the Cambridge Philosophical Society · 2026Review
- Dissecting the Molecular Regulation of Natural Variation in Growth and Senescence of TwoInternational journal of molecular sciences · 2022Article
- Tandem Mass Tagging (TMT) Reveals Tissue-Specific Proteome of L4 Larvae ofInternational journal of molecular sciences · 2022Article
- Comparison of gut microflora of donkeys in high and low altitude areas.Frontiers in microbiology · 2022Article
- The dual role of SrbA from Paracoccidioides lutzii: a hypoxic regulator.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2021Article
- Using Linear Discriminant Analysis to Characterize Novel Single Nucleotide Polymorphisms and Expression Profile Changes in Genes of Three Breeds of Rabbit (Comparative medicine · 2021Article
- The Protein Interactome of Glycolysis inProteomes · 2021Article
- Glucose Metabolism and Acetate Switch in Archaea: the Enzymes in Haloferax volcanii.Journal of bacteriology · 2021Article
- Physiological and Proteomic Analyses of Molybdenum- and Ethylene-Responsive Mechanisms in Rubber Latex.Frontiers in plant science · 2018Article
- The complete genome sequence and emendation of the hyperthermophilic, obligate iron-reducing archaeon "Geoglobus ahangari" strain 234(T).Standards in genomic sciences · 2015Article
- Regulation of Cadmium-Induced Proteomic and Metabolic Changes by 5-Aminolevulinic Acid in Leaves of Brassica napus L.PloS one · 2015Article
- Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.Microbiology and molecular biology reviews : MMBR · 2014Review
- Cofactor independent phosphoglycerate mutase of Brugia malayi induces a mixed Th1/Th2 type immune response and inhibits larval development in the host.BioMed research international · 2014Article
- Substrate ambiguous enzymes within the Escherichia coli proteome offer different evolutionary solutions to the same problem.Molecular biology and evolution · 2013Article
- Synthetic metabolic engineering-a novel, simple technology for designing a chimeric metabolic pathway.Microbial cell factories · 2012Article
- Article
- The Wolbachia endosymbiont of Brugia malayi has an active phosphoglycerate mutase: a candidate target for anti-filarial therapies.Parasitology research · 2009Article
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphoglycerate mutases (PGM) catalyze the reversible conversion of 3-phosphoglycerate and 2-phosphoglycerate as part of glycolysis and gluconeogenesis. Two structural and mechanistically unrelated types of PGMs are known, a cofactor (2,3-bisphosphoglycerate)-dependent (dPGM) and a cofactor-independent enzyme (iPGM). Here, we report the characterization of the first archaeal cofactor-dependent PGM from Thermoplasma acidophilum, which is encoded by ORF TA1347. This ORF was cloned and expressed in Escherichia coli and the recombinant protein was characterized as functional dPGM. The enzyme constitutes a 46 kDa homodimeric protein. Enzyme activity required 2,3-bisphosphoglycerate as cofactor and was inhibited by vanadate, a specific inhibitor of dPGMs in bacteria and eukarya; inhibition could be partially relieved by EDTA. Histidine 23 of the archaeal dPGM of T. acidophilum, which corresponds to active site histidine in dPGMs from bacteria and eukarya, was exchanged for alanine by site directed mutagenesis. The H23A mutant was catalytically inactive supporting the essential role of H23 in catalysis of the archaeal dPGM. Further, an archaeal cofactor-independent PGM encoded by ORF AF1751 from the hyperthermophilic sulfate reducer Archaeoglobus fulgidus was characterized after expression in E. coli. The monomeric 46 kDa protein showed cofactor-independent PGM activity and was stimulated by Mn(2+) and exhibited high thermostability up to 70 degrees C. A comprehensive phylogenetic analysis of both types of archaeal phosphoglycerate mutases is also presented.
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