NDLI: Characterization of cofactor-dependent and cofactor-independent phosphoglycerate mutases from Archaea

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Characterization of cofactor-dependent and cofactor-independent phosphoglycerate mutases from Archaea

Content Provider	Springer Nature Link
Author	Johnsen, Ulrike Schönheit, Peter
Copyright Year	2007
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 Mn2+ and exhibited high thermostability up to 70°C. A comprehensive phylogenetic analysis of both types of archaeal phosphoglycerate mutases is also presented.
Starting Page	647
Ending Page	657
Page Count	11
File Format	PDF
ISSN	14310651
Journal	Extremophiles
Volume Number	11
Issue Number	5
e-ISSN	14334909
Language	English
Publisher	Springer-Verlag
Publisher Date	2007-06-19
Publisher Place	Tokyo
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Phosphoglycerate mutases Archaea Thermoplasma acidophilum Archaeoglobus fulgidus Ecology Biotechnology Microbiology
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Medicine Microbiology

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